1qu0
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1qu0 |SIZE=350|CAPTION= <scene name='initialview01'>1qu0</scene>, resolution 2.35Å | |PDB= 1qu0 |SIZE=350|CAPTION= <scene name='initialview01'>1qu0</scene>, resolution 2.35Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qu0 OCA], [http://www.ebi.ac.uk/pdbsum/1qu0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qu0 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
[[Category: Tisi, D.]] | [[Category: Tisi, D.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: SO4]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:58 2008'' |
Revision as of 20:18, 30 March 2008
| |||||||
| , resolution 2.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 23:18:58 2008
