1vfq: Difference between revisions

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[[Image:1vfq.~~gif~~|left|200px]]

[[Image:1vfq.png|left|200px]]

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~~'''~~The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution~~'''~~

===The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution===

~~==Overview==~~

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~~Human coactosin~~-~~like protein (CLP) shares high homology with coactosin, a filamentous (F)~~-~~actin binding protein~~, ~~and interacts with 5LO and F-actin. As a tumor antigen~~, ~~CLP is overexpressed in tumor tissue cells or cell lines, and~~ the ~~encoded epitopes can be recognized by cellular and humoral immune systems. To gain a better understanding of its various functions and interactions with related proteins,~~ the ~~crystal structure of CLP expressed in Escherichia coli has been determined to 1~~.~~9 A resolution~~. ~~The structure features a central beta-sheet surrounded by helices~~, ~~with two very tight hydrophobic cores on each side of~~ the ~~sheet~~. CLP belongs to the actin depolymerizing protein superfamily, and is similar to yeast cofilin and actophilin. Based on our structural analysis, we observed that CLP forms a polymer along the crystallographic b axis with the exact same repeat distance as F-~~actin. A model for the CLP polymer and F~~-~~actin binding has therefore been proposed.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15459340}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15459340 is the PubMed ID number.

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==About this Structure==

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[[Category: Actin-binding protein]]

[[Category: Cytoskeleton]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 12~~:29~~:28~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:10:29 2008''

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-[[Image:1vfq.gif|left|200px]]
+{{Seed}}
+[[Image:1vfq.png|left|200px]]
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 {{STRUCTURE_1vfq|  PDB=1vfq  |  SCENE=  }}
-'''The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution'''
+===The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution===
-==Overview==
+<!--
-Human coactosin-like protein (CLP) shares high homology with coactosin, a filamentous (F)-actin binding protein, and interacts with 5LO and F-actin. As a tumor antigen, CLP is overexpressed in tumor tissue cells or cell lines, and the encoded epitopes can be recognized by cellular and humoral immune systems. To gain a better understanding of its various functions and interactions with related proteins, the crystal structure of CLP expressed in Escherichia coli has been determined to 1.9 A resolution. The structure features a central beta-sheet surrounded by helices, with two very tight hydrophobic cores on each side of the sheet. CLP belongs to the actin depolymerizing protein superfamily, and is similar to yeast cofilin and actophilin. Based on our structural analysis, we observed that CLP forms a polymer along the crystallographic b axis with the exact same repeat distance as F-actin. A model for the CLP polymer and F-actin binding has therefore been proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_15459340}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15459340 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15459340}}
 ==About this Structure==
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 [[Category: Actin-binding protein]]
 [[Category: Cytoskeleton]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:29:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:10:29 2008''