1dyk
From Proteopedia
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LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR
Overview
The laminins are large heterotrimeric glycoproteins with fundamental roles, in basement membrane architecture and function. The C-terminus of the, laminin alpha chain contains a tandem of five laminin G-like (LG) domains., We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain, pair, which harbours binding sites for heparin and the cell surface, receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3, fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110, degrees rotation about an axis passing near the domain termini. An, extended N-terminal segment is disulfide bonded to LG5 and stabilizes the, domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A, apart at the tips of the domains opposite the polypeptide termini. An, extensive basic surface region between the calcium sites is proposed to, bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to, construct a model of the laminin LG1-LG5 tandem and interpret missense, mutations underlying protein S deficiency.
About this Structure
1DYK is a Single protein structure of sequence from Mus musculus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin., Tisi D, Talts JF, Timpl R, Hohenester E, EMBO J. 2000 Apr 3;19(7):1432-40. PMID:10747011
Page seeded by OCA on Tue Nov 20 13:41:05 2007
Categories: Mus musculus | Single protein | Hohenester, E. | Talts, J.F. | Timple, R. | Tisi, D. | CA | Laminin
