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1hci
From Proteopedia
(New page: 200px<br /> <applet load="1hci" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hci, resolution 2.80Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1hci.gif|left|200px]]<br /> | + | [[Image:1hci.gif|left|200px]]<br /><applet load="1hci" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hci" size=" | + | |
caption="1hci, resolution 2.80Å" /> | caption="1hci, resolution 2.80Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ'''<br /> | '''CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Alpha-actinin is a ubiquitously expressed protein found in | + | BACKGROUND: Alpha-actinin is a ubiquitously expressed protein found in numerous actin structures. It consists of an N-terminal actin binding domain, a central rod domain, and a C-terminal domain and functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins. RESULTS: We report here the crystal structure of the alpha-actinin rod. The structure is a twisted antiparallel dimer that contains a conserved acidic surface. CONCLUSIONS: The novel features revealed by the structure allow prediction of the orientation of parallel and antiparallel cross-linked actin filaments in relation to alpha-actinin. The conserved acidic surface is a possible interaction site for several cytoplasmic tails of transmembrane proteins involved in the recruitment of alpha-actinin to the plasma membrane. |
==About this Structure== | ==About this Structure== | ||
| - | 1HCI 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:// | + | 1HCI 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=1HCI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: z-line]] | [[Category: z-line]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:47 2008'' |
Revision as of 10:59, 21 February 2008
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CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ
Overview
BACKGROUND: Alpha-actinin is a ubiquitously expressed protein found in numerous actin structures. It consists of an N-terminal actin binding domain, a central rod domain, and a C-terminal domain and functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins. RESULTS: We report here the crystal structure of the alpha-actinin rod. The structure is a twisted antiparallel dimer that contains a conserved acidic surface. CONCLUSIONS: The novel features revealed by the structure allow prediction of the orientation of parallel and antiparallel cross-linked actin filaments in relation to alpha-actinin. The conserved acidic surface is a possible interaction site for several cytoplasmic tails of transmembrane proteins involved in the recruitment of alpha-actinin to the plasma membrane.
About this Structure
1HCI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the alpha-actinin rod reveals an extensive torsional twist., Ylanne J, Scheffzek K, Young P, Saraste M, Structure. 2001 Jul 3;9(7):597-604. PMID:11470434
Page seeded by OCA on Thu Feb 21 12:59:47 2008
