2bve: Difference between revisions

Revision as of 04:13, 28 July 2008

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File:2bve.png

Template:STRUCTURE 2bve

STRUCTURE OF THE N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH 2-PHENYL-PROP5ACSTRUCTURE OF THE N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH 2-PHENYL-PROP5AC

Template:ABSTRACT PUBMED 17137591

About this StructureAbout this Structure

2BVE is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin., Zaccai NR, May AP, Robinson RC, Burtnick LD, Crocker PR, Brossmer R, Kelm S, Jones EY, J Mol Biol. 2007 Feb 2;365(5):1469-79. Epub 2006 Oct 28. PMID:17137591

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURE OF THE N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH 2-PHENYL-PROP5AC'''
+===STRUCTURE OF THE N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH 2-PHENYL-PROP5AC===
-==Overview==
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-The Siglec family of receptors mediates cell-surface interactions through recognition of sialylated glycoconjugates. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. To characterize further the carbohydrate-binding properties, we have determined the crystal structures of SnD1 in the absence of ligand, and in complex with 2-benzyl-Neu5NPro and 2-benzyl-Neu5NAc. These structures reveal that SnD1 undergoes very few structural changes on ligand binding and detail how two novel classes of sialic acid analogs bind, one of which unexpectedly can induce Siglec dimerization. In conjunction with in silico analysis, this set of structures informs us about the design of putative ligands with enhanced binding affinities and specificities to different Siglecs, and provides data with which to test the effectiveness of different computational drug design protocols.
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 [[Category: Inhibitor design]]
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