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1xph
From Proteopedia
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(New page: 200px<br /> <applet load="1xph" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xph, resolution 1.41Å" /> '''Structure of DC-SIG...)
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Revision as of 18:02, 12 November 2007
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Structure of DC-SIGNR and a portion of repeat domain 8
Contents |
Overview
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.
Disease
Known disease associated with this structure: SARS infection, protection against OMIM:[605872]
About this Structure
1XPH is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.
Reference
The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer., Snyder GA, Colonna M, Sun PD, J Mol Biol. 2005 Apr 15;347(5):979-89. PMID:15784257
Page seeded by OCA on Mon Nov 12 20:09:19 2007
