1qu0: Difference between revisions

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[[Image:1qu0.jpg|left|200px]]<br /><applet load="1qu0" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1qu0.jpg|left|200px]]
caption="1qu0, resolution 2.35&Aring;" />
 
'''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN'''<br />
{{Structure
|PDB= 1qu0 |SIZE=350|CAPTION= <scene name='initialview01'>1qu0</scene>, resolution 2.35&Aring;
|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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU0 OCA].  
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10619025 10619025]
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 Feb 21 14:43:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:42:43 2008''

Revision as of 14:42, 20 March 2008

File:1qu0.jpg


PDB ID 1qu0

Drag the structure with the mouse to rotate
, resolution 2.35Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN


OverviewOverview

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 StructureAbout this Structure

1QU0 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

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