1by2

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(New page: 200px<br /> <applet load="1by2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by2, resolution 2.00&Aring;" /> '''STRUCTURE OF M2BP S...)
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Revision as of 14:08, 12 November 2007


1by2, resolution 2.00Å

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STRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN

Overview

Scavenger receptor cysteine-rich (SRCR) domains are found widely in cell, surface molecules and in some secreted proteins, where they are thought to, mediate ligand binding. We have determined the crystal structure at 2.0 A, resolution of the SRCR domain of Mac-2 binding protein (M2BP), a, tumor-associated antigen and matrix protein. The structure reveals a, curved six-stranded beta-sheet cradling an alpha-helix. Structure-based, sequence alignment demonstrates that the M2BP SRCR domain is a valid, template for the entire SRCR protein superfamily. This allows an, interpretation of previous mutagenesis data on ligand binding to the, lymphocyte receptor CD6.

About this Structure

1BY2 is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily., Hohenester E, Sasaki T, Timpl R, Nat Struct Biol. 1999 Mar;6(3):228-32. PMID:10074941

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