1okq
From Proteopedia
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'''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR, CA1 SITE MUTANT''' | '''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR, CA1 SITE MUTANT''' | ||
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[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
[[Category: Wizemann, H.]] | [[Category: Wizemann, H.]] | ||
| - | [[Category: | + | [[Category: Laminin]] |
| - | [[Category: | + | [[Category: Metal binding protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:58:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:58, 3 May 2008
LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR, CA1 SITE MUTANT
Overview
Laminin-2 (alpha2beta1gamma1) is found in basement membranes surrounding muscle and peripheral nerve cells. Several types of cellular receptors bind to the laminin G-like (LG) domains at the C terminus of the alpha2 chain, the interaction with alpha-dystroglycan (alpha-DG) being particularly important in muscle. We have used site-directed mutagenesis and in vitro binding assays to map the binding sites on the laminin alpha2 chain LG4-LG5 domain pair for alpha-DG, heparin and sulfatides. Calcium-dependent alpha-DG recognition requires the calcium ion in LG4, but not the one in LG5, as well as basic residues in both LG domains. Heparin and sulfatides also bind to basic residues in both LG domains, but there is little overlap in the binding sites for alpha-DG and heparin/sulfatides. The results should prove useful for the molecular dissection of laminin-receptor interactions in vivo.
About this Structure
1OKQ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Distinct requirements for heparin and alpha-dystroglycan binding revealed by structure-based mutagenesis of the laminin alpha2 LG4-LG5 domain pair., Wizemann H, Garbe JH, Friedrich MV, Timpl R, Sasaki T, Hohenester E, J Mol Biol. 2003 Sep 19;332(3):635-42. PMID:12963372 Page seeded by OCA on Sat May 3 03:58:33 2008
