Research graph
References from Druggable secondary sites in C-type lectin-like domains: Mechanistic insights and opportunities for chemical modulation. Local targets link to admitted publications; unresolved targets remain external evidence.
UniLectin3D, a database of carbohydrate binding proteins with curated information on 3D structures and interacting ligands
10.1093/nar/gky832 · 2019 · External reference
C-type lectins in immunity and homeostasis
10.1038/s41577-018-0004-8 · 2018 · External reference
Biological roles of glycans
10.1093/glycob/cww086 · 2017 · External reference
C-Type lectins
2022 · External reference
The C-type lectin-like domain superfamily
10.1111/j.1742-4658.2005.05031.x · 2005 · External reference
Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities
10.1093/glycob/cwq193 · 2011 · External reference
Secondary sites of the C-type lectin-like fold
10.1002/chem.202400660 · 2024 · External reference
What contributes to an effective mannose recognition domain?
10.3762/bjoc.13.255 · 2017 · External reference
Glycomimetics for the inhibition and modulation of lectins
10.1039/d2cs00954d · 2023 · External reference
Allostery in C-type lectins
10.1016/j.sbi.2019.11.003 · 2020 · External reference
Identification of multiple druggable secondary sites by fragment screening against DC-SIGN
10.1002/anie.201701943 · 2017 · External reference
A remote secondary binding pocket promotes heteromultivalent targeting of DC-SIGN
10.1021/jacs.1c07235 · 2021 · External reference
Allosteric inhibition of a Mammalian lectin
10.1021/jacs.8b08644 · 2018 · External reference
Cryptic binding sites on proteins: definition, detection, and druggability
10.1016/j.cbpa.2018.05.003 · 2018 · External reference
Binding-site geometry and flexibility in DC-SIGN demonstrated with surface force measurements
10.1073/pnas.0901783106 · 2009 · External reference
Powerful avidity with a limited valency for virus-attachment blockers on DC-SIGN: combining chelation and statistical rebinding with structural plasticity of the receptor
10.1021/acscentsci.2c01136 · 2023 · External reference
DC-SIGN, a dendritic cell–specific HIV-1-Binding protein that enhances trans-Infection of T cells
10.1016/s0092-8674(00)80694-7 · 2000 · External reference
Aryl fucosides: synthesis and evaluation of their binding affinity towards the DC-SIGN receptor
10.1039/d5ob00472a · 2025 · External reference
A cryptic pocket allosterically modulates oligosaccharide binding to DC-SIGN
10.1021/jacsau.5c01465 · 2026 · External reference
Engagement of a neighboring lys residue by a salicylaldehyde-modified glycomimetic ligand enables potent and selective binding to DC-SIGN over L-SIGN
10.1002/ceur.202500485 · 2026 · External reference
Covalent activation of the C-type Lectin DC-SIGN
10.1002/anie.202520594 · 2026 · External reference
Structural basis for Langerin recognition of diverse pathogen and Mammalian glycans through a single binding site
10.1016/j.jmb.2010.11.039 · 2011 · External reference
A specific, glycomimetic Langerin ligand for human langerhans cell targeting
10.1021/acscentsci.9b00093 · 2019 · External reference
Anomeric configuration of a glycomimetic ligand tunes cross-species targeted delivery to Langerhans cells
2026 · External reference
Identification of the allosteric binding site for thiazolopyrimidine on the C-Type lectin langerin
10.1021/acschembio.2c00626 · 2022 · External reference
Calcium competitive inhibition of Langerin by thiazolopyrimidinones
10.1021/acs.jmedchem.5c01756 · 2025 · External reference
Roles of the NKG2D immunoreceptor and its ligands
10.1038/nri1199 · 2003 · External reference
Development of small molecule inhibitors of natural killer group 2D receptor (NKG2D)
10.1016/j.bmcl.2023.129492 · 2023 · External reference
Complex structure of the activating immunoreceptor NKG2D and its MHC class I–like ligand MICA
10.1038/87757 · 2001 · External reference
Identification of small-molecule protein–protein interaction inhibitors for NKG2D
10.1073/pnas.2216342120 · 2023 · External reference
Structure-based design targeted at LOX-1, a receptor for oxidized low-density lipoprotein
10.1038/srep16740 · 2015 · External reference
A small-molecule inhibitor of lectin-like oxidized LDL receptor-1 acts by stabilizing an inactive receptor tetramer state
10.1038/s42004-020-0321-2 · 2020 · External reference
Exploring the druggability of oxidized low-density lipoprotein (ox-LDL) receptor, LOX-1, a proatherogenic drug target involved in atherosclerosis
10.1016/j.bbrc.2022.07.036 · 2022 · External reference
Crystal structure of Human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL
10.1016/j.str.2005.03.016 · 2005 · External reference
Identification of a secondary binding site in human macrophage galactose-type lectin by microarray studies: implications for the molecular recognition of its ligands
10.1074/jbc.ra118.004957 · 2019 · External reference
The plasticity of the carbohydrate recognition domain dictates the exquisite mechanism of binding of human macrophage galactose-type lectin
10.1002/chem.201902780 · 2019 · External reference
The unique 3D arrangement of macrophage galactose lectin enables Escherichia coli lipopolysaccharide recognition through two distinct interfaces
10.1093/pnasnexus/pgad310 · 2023 · External reference
The mannose receptor: from endocytic receptor and biomarker to regulator of (Meta)Inflammation
10.3389/fimmu.2021.765034 · 2021 · External reference
The mannose receptor family
10.1016/s0304-4165(02)00319-7 · 2002 · External reference
Characterization of ligand binding to a carbohydrate-recognition domain of the macrophage mannose receptor
10.1016/s0021-9258(18)46942-6 · 1994 · External reference
Structural basis of the pH-dependent conformational change of the N-terminal region of human mannose receptor/CD206
10.1016/j.jsb.2019.09.001 · 2019 · External reference
Deglycosylation induces a novel distal conformation in the mannose receptor CD206
10.1038/s41598-026-35240-y · 2026 · External reference
Mannose receptor (CD206) activation in tumor-associated macrophages enhances adaptive and innate antitumor immune responses
10.1126/scitranslmed.aax6337 · 2020 · External reference
Precision targeting of tumor macrophages with a CD206 binding peptide
10.1038/s41598-017-14709-x · 2017 · External reference
Peptide-Drug conjugate for therapeutic reprogramming of tumor-associated macrophages in breast cancer
10.1002/advs.202410288 · 2025 · External reference
The cryo-EM structure of the endocytic receptor DEC-205
10.1074/jbc.ra120.016451 · 2021 · External reference
Crystal structures of the ligand-binding region of uPARAP: effect of calcium ion binding
10.1042/bcj20160276 · 2016 · External reference
The molecular basis for the pH-dependent calcium affinity of the pattern recognition receptor langerin
10.1016/j.jbc.2021.100718 · 2021 · External reference
Dectin-1: a signalling non-TLR pattern-recognition receptor
10.1038/nri1745 · 2006 · External reference
Langerhans cell-targeted protein delivery enhances antigen-specific cellular immune response
10.1016/j.ymthe.2025.10.008 · 2026 · External reference
Peptide-Drug conjugate for therapeutic reprogramming of tumor-associated macrophages in breast cancer
10.1002/advs.202410288 · ExternalCitation · doi-reference
Identification of multiple druggable secondary sites by fragment screening against DC-SIGN
10.1002/anie.201701943 · ExternalCitation · doi-reference
Covalent activation of the C-type Lectin DC-SIGN
10.1002/anie.202520594 · ExternalCitation · doi-reference
Engagement of a neighboring lys residue by a salicylaldehyde-modified glycomimetic ligand enables potent and selective binding to DC-SIGN over L-SIGN
10.1002/ceur.202500485 · ExternalCitation · doi-reference
The plasticity of the carbohydrate recognition domain dictates the exquisite mechanism of binding of human macrophage galactose-type lectin
10.1002/chem.201902780 · ExternalCitation · doi-reference
Secondary sites of the C-type lectin-like fold
10.1002/chem.202400660 · ExternalCitation · doi-reference
Exploring the druggability of oxidized low-density lipoprotein (ox-LDL) receptor, LOX-1, a proatherogenic drug target involved in atherosclerosis
10.1016/j.bbrc.2022.07.036 · ExternalCitation · doi-reference
Development of small molecule inhibitors of natural killer group 2D receptor (NKG2D)
10.1016/j.bmcl.2023.129492 · ExternalCitation · doi-reference
Cryptic binding sites on proteins: definition, detection, and druggability
10.1016/j.cbpa.2018.05.003 · ExternalCitation · doi-reference
The molecular basis for the pH-dependent calcium affinity of the pattern recognition receptor langerin
10.1016/j.jbc.2021.100718 · ExternalCitation · doi-reference
Structural basis for Langerin recognition of diverse pathogen and Mammalian glycans through a single binding site
10.1016/j.jmb.2010.11.039 · ExternalCitation · doi-reference
Structural basis of the pH-dependent conformational change of the N-terminal region of human mannose receptor/CD206
10.1016/j.jsb.2019.09.001 · ExternalCitation · doi-reference
Allostery in C-type lectins
10.1016/j.sbi.2019.11.003 · ExternalCitation · doi-reference
Crystal structure of Human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL
10.1016/j.str.2005.03.016 · ExternalCitation · doi-reference
Langerhans cell-targeted protein delivery enhances antigen-specific cellular immune response
10.1016/j.ymthe.2025.10.008 · ExternalCitation · doi-reference
Characterization of ligand binding to a carbohydrate-recognition domain of the macrophage mannose receptor
10.1016/s0021-9258(18)46942-6 · ExternalCitation · doi-reference
DC-SIGN, a dendritic cell–specific HIV-1-Binding protein that enhances trans-Infection of T cells
10.1016/s0092-8674(00)80694-7 · ExternalCitation · doi-reference
The mannose receptor family
10.1016/s0304-4165(02)00319-7 · ExternalCitation · doi-reference
Calcium competitive inhibition of Langerin by thiazolopyrimidinones
10.1021/acs.jmedchem.5c01756 · ExternalCitation · doi-reference
Powerful avidity with a limited valency for virus-attachment blockers on DC-SIGN: combining chelation and statistical rebinding with structural plasticity of the receptor
10.1021/acscentsci.2c01136 · ExternalCitation · doi-reference
A specific, glycomimetic Langerin ligand for human langerhans cell targeting
10.1021/acscentsci.9b00093 · ExternalCitation · doi-reference
Identification of the allosteric binding site for thiazolopyrimidine on the C-Type lectin langerin
10.1021/acschembio.2c00626 · ExternalCitation · doi-reference
A remote secondary binding pocket promotes heteromultivalent targeting of DC-SIGN
10.1021/jacs.1c07235 · ExternalCitation · doi-reference
Allosteric inhibition of a Mammalian lectin
10.1021/jacs.8b08644 · ExternalCitation · doi-reference
A cryptic pocket allosterically modulates oligosaccharide binding to DC-SIGN
10.1021/jacsau.5c01465 · ExternalCitation · doi-reference
Complex structure of the activating immunoreceptor NKG2D and its MHC class I–like ligand MICA
10.1038/87757 · ExternalCitation · doi-reference
Roles of the NKG2D immunoreceptor and its ligands
10.1038/nri1199 · ExternalCitation · doi-reference
Dectin-1: a signalling non-TLR pattern-recognition receptor
10.1038/nri1745 · ExternalCitation · doi-reference
C-type lectins in immunity and homeostasis
10.1038/s41577-018-0004-8 · ExternalCitation · doi-reference
Precision targeting of tumor macrophages with a CD206 binding peptide
10.1038/s41598-017-14709-x · ExternalCitation · doi-reference
Deglycosylation induces a novel distal conformation in the mannose receptor CD206
10.1038/s41598-026-35240-y · ExternalCitation · doi-reference
A small-molecule inhibitor of lectin-like oxidized LDL receptor-1 acts by stabilizing an inactive receptor tetramer state
10.1038/s42004-020-0321-2 · ExternalCitation · doi-reference
Structure-based design targeted at LOX-1, a receptor for oxidized low-density lipoprotein
10.1038/srep16740 · ExternalCitation · doi-reference
Glycomimetics for the inhibition and modulation of lectins
10.1039/d2cs00954d · ExternalCitation · doi-reference
Aryl fucosides: synthesis and evaluation of their binding affinity towards the DC-SIGN receptor
10.1039/d5ob00472a · ExternalCitation · doi-reference
Crystal structures of the ligand-binding region of uPARAP: effect of calcium ion binding
10.1042/bcj20160276 · ExternalCitation · doi-reference
Binding-site geometry and flexibility in DC-SIGN demonstrated with surface force measurements
10.1073/pnas.0901783106 · ExternalCitation · doi-reference
Identification of small-molecule protein–protein interaction inhibitors for NKG2D
10.1073/pnas.2216342120 · ExternalCitation · doi-reference
Identification of a secondary binding site in human macrophage galactose-type lectin by microarray studies: implications for the molecular recognition of its ligands
10.1074/jbc.ra118.004957 · ExternalCitation · doi-reference
The cryo-EM structure of the endocytic receptor DEC-205
10.1074/jbc.ra120.016451 · ExternalCitation · doi-reference
Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities
10.1093/glycob/cwq193 · ExternalCitation · doi-reference
Biological roles of glycans
10.1093/glycob/cww086 · ExternalCitation · doi-reference
UniLectin3D, a database of carbohydrate binding proteins with curated information on 3D structures and interacting ligands
10.1093/nar/gky832 · ExternalCitation · doi-reference
The unique 3D arrangement of macrophage galactose lectin enables Escherichia coli lipopolysaccharide recognition through two distinct interfaces
10.1093/pnasnexus/pgad310 · ExternalCitation · doi-reference
The C-type lectin-like domain superfamily
10.1111/j.1742-4658.2005.05031.x · ExternalCitation · doi-reference
Mannose receptor (CD206) activation in tumor-associated macrophages enhances adaptive and innate antitumor immune responses
10.1126/scitranslmed.aax6337 · ExternalCitation · doi-reference
The mannose receptor: from endocytic receptor and biomarker to regulator of (Meta)Inflammation
10.3389/fimmu.2021.765034 · ExternalCitation · doi-reference
What contributes to an effective mannose recognition domain?
10.3762/bjoc.13.255 · ExternalCitation · doi-reference
