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| {{STRUCTURE_1xph| PDB=1xph | SCENE= }} | | {{STRUCTURE_1xph| PDB=1xph | SCENE= }} |
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| '''Structure of DC-SIGNR and a portion of repeat domain 8'''
| | ===Structure of DC-SIGNR and a portion of repeat domain 8=== |
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| ==Overview==
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| The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close relative DC-SIGNR recognize various glycoproteins, both pathogenic and cellular, through the receptor lectin domain-mediated carbohydrate recognition. While the carbohydrate-recognition domains (CRD) exist as monomers and bind individual carbohydrates with low affinity and are permissive in nature, the full-length receptors form tetramers through their repeat domain and recognize specific ligands with high affinity. To understand the tetramer-based ligand binding avidity, we determined the crystal structure of DC-SIGNR with its last repeat region. Compared to the carbohydrate-bound CRD structure, the structure revealed conformational changes in the calcium and carbohydrate coordination loops of CRD, an additional disulfide bond between the N and the C termini of the CRD, and a helical conformation for the last repeat. On the basis of the current crystal structure and other published structures with sequence homology to the repeat domain, we generated a tetramer model for DC-SIGN/R using homology modeling and propose a ligand-recognition index to identify potential receptor ligands. | | The line below this paragraph, {{ABSTRACT_PUBMED_15784257}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15784257 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15784257}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Carbohydrate recognition domain]] | | [[Category: Carbohydrate recognition domain]] |
| [[Category: Repeat domain]] | | [[Category: Repeat domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:20:03 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:19:18 2008'' |
