1qu0
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(New page: 200px<br /><applet load="1qu0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qu0, resolution 2.35Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 22:51, 20 November 2007
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CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN
Overview
Laminin G-like (LG) modules in the extracellular matrix glycoproteins, laminin, perlecan, and agrin mediate the binding to heparin and the cell, surface receptor alpha-dystroglycan (alpha-DG). These interactions are, crucial to basement membrane assembly, as well as muscle and nerve cell, function. The crystal structure of the laminin alpha 2 chain LG5 module, reveals a 14-stranded beta sandwich. A calcium ion is bound to one edge of, the sandwich by conserved acidic residues and is surrounded by residues, implicated in heparin and alpha-DG binding. A calcium-coordinated sulfate, ion is suggested to mimic the binding of anionic oligosaccharides. The, structure demonstrates a conserved function of the LG module in, calcium-dependent lectin-like alpha-DG binding.
About this Structure
1QU0 is a Single protein structure of sequence from Mus musculus with CA and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin., Hohenester E, Tisi D, Talts JF, Timpl R, Mol Cell. 1999 Nov;4(5):783-92. PMID:10619025
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