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1xph
From Proteopedia
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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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[[Category: Snyder, G A.]] | [[Category: Snyder, G A.]] | ||
[[Category: Sun, P D.]] | [[Category: Sun, P D.]] | ||
| - | [[Category: | + | [[Category: C-type lectin]] |
| - | [[Category: | + | [[Category: Carbohydrate recognition domain]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 12:20, 3 May 2008
Structure of DC-SIGNR and a portion of repeat domain 8
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.
About this Structure
1XPH is a Single protein structure of sequence from Homo sapiens. 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 Sat May 3 15:20:03 2008
