2v5m | pdb_00002v5m

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Revision as of 20:59, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2v5m" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v5m, resolution 1.95Å" /> '''STRUCTURAL BASIS FO...)
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STRUCTURAL BASIS FOR DSCAM ISOFORM SPECIFICITY

File:2v5m.gif


2v5m, resolution 1.95Å

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Overview

The Dscam gene gives rise to thousands of diverse cell surface receptors, thought to provide homophilic and heterophilic recognition specificity for, neuronal wiring and immune responses. Mutually exclusive splicing allows, for the generation of sequence variability in three immunoglobulin, ecto-domains, D2, D3 and D7. We report X-ray structures of the, amino-terminal four immunoglobulin domains (D1-D4) of two distinct Dscam, isoforms. The structures reveal a horseshoe configuration, with variable, residues of D2 and D3 constituting two independent surface epitopes on, either side of the receptor. Both isoforms engage in homo-dimerization, coupling variable domain D2 with D2, and D3 with D3. These interactions, involve symmetric, antiparallel pairing of identical peptide segments from, ... [(full description)]

About this Structure

2V5M is a [Single protein] structure of sequence from [Drosophila melanogaster] with GOL as [ligand]. Full crystallographic information is available from [OCA].

Reference

Structural basis of Dscam isoform specificity., Meijers R, Puettmann-Holgado R, Skiniotis G, Liu JH, Walz T, Wang JH, Schmucker D, Nature. 2007 Aug 26;. PMID:17721508

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