1dyk: Difference between revisions
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[[Image:1dyk.gif|left|200px]] | [[Image:1dyk.gif|left|200px]] | ||
'''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR''' | {{Structure | ||
|PDB= 1dyk |SIZE=350|CAPTION= <scene name='initialview01'>1dyk</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DYK is a [ | 1DYK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYK OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10747011 10747011] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: laminin]] | [[Category: laminin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:46:39 2008'' | ||
Revision as of 08:46, 20 March 2008
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| 1dyk, resolution 2.00Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
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