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'''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN''' | '''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN''' | ||
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[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
[[Category: Tisi, D.]] | [[Category: Tisi, D.]] | ||
[[Category: | [[Category: Beta sandwich]] | ||
[[Category: | [[Category: Calcium-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:42:16 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:42, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 06:42:16 2008
