1xph
From Proteopedia
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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 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 Thu Feb 21 15:57:14 2008
