1qu0
From Proteopedia
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| - | [[Image:1qu0.jpg|left|200px]] | + | [[Image:1qu0.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN''' | + | {{Structure |
| + | |PDB= 1qu0 |SIZE=350|CAPTION= <scene name='initialview01'>1qu0</scene>, resolution 2.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QU0 is a [ | + | 1QU0 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=1QU0 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10619025 10619025] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''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 13:42:43 2008'' |
Revision as of 11:42, 20 March 2008
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| , resolution 2.35Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:42:43 2008
