1quu
From Proteopedia
(New page: 200px<br /> <applet load="1quu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1quu, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1quu.gif|left|200px]]<br /> | + | [[Image:1quu.gif|left|200px]]<br /><applet load="1quu" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1quu" size=" | + | |
caption="1quu, resolution 2.5Å" /> | caption="1quu, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ'''<br /> | '''CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the crystal structure of the two central repeats in the | + | We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments. |
==About this Structure== | ==About this Structure== | ||
| - | 1QUU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1QUU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: triple-helix coiled coil]] | [[Category: triple-helix coiled coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:57 2008'' |
Revision as of 12:43, 21 February 2008
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CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ
Overview
We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments.
About this Structure
1QUU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments., Djinovic-Carugo K, Young P, Gautel M, Saraste M, Cell. 1999 Aug 20;98(4):537-46. PMID:10481917
Page seeded by OCA on Thu Feb 21 14:43:57 2008
