1qu0

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[[Image:1qu0.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1qu0| PDB=1qu0 | SCENE= }}
{{STRUCTURE_1qu0| PDB=1qu0 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN'''
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===CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_10619025}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10619025 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10619025}}
==About this Structure==
==About this Structure==
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[[Category: Beta sandwich]]
[[Category: Beta sandwich]]
[[Category: Calcium-binding protein]]
[[Category: Calcium-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:42:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:55:26 2008''

Revision as of 12:55, 29 July 2008

Image:1qu0.png

Template:STRUCTURE 1qu0

CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN

Template:ABSTRACT PUBMED 10619025

About this Structure

1QU0 is a Single protein structure of sequence from Mus musculus. 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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