1qu0: Difference between revisions
New page: left|200px<br /><applet load="1qu0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qu0, resolution 2.35Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1qu0.jpg|left|200px]]<br /><applet load="1qu0" size=" | [[Image:1qu0.jpg|left|200px]]<br /><applet load="1qu0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1qu0, resolution 2.35Å" /> | caption="1qu0, resolution 2.35Å" /> | ||
'''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN'''<br /> | ||
==Overview== | ==Overview== | ||
Laminin G-like (LG) modules in the extracellular matrix glycoproteins | 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== | ==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 CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
[[Category: Talts, J | [[Category: Talts, J F.]] | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
[[Category: Tisi, D.]] | [[Category: Tisi, D.]] | ||
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[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:43 2008'' | ||
Revision as of 12:43, 21 February 2008
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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 with CA and SO4 as ligands. 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
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