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| [[Image:1dyk.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1dyk| PDB=1dyk | SCENE= }} | | {{STRUCTURE_1dyk| PDB=1dyk | SCENE= }} |
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| '''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR'''
| | ===LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10747011}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10747011 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10747011}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tisi, D.]] | | [[Category: Tisi, D.]] |
| [[Category: Laminin]] | | [[Category: Laminin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:26:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:48:52 2008'' |
