Structural highlights
Function
[COTL1_HUMAN] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of human coactosin-like protein at 1.9 A resolution.,Li X, Liu X, Lou Z, Duan X, Wu H, Liu Y, Rao Z Protein Sci. 2004 Nov;13(11):2845-51. Epub 2004 Sep 30. PMID:15459340[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Provost P, Doucet J, Stock A, Gerisch G, Samuelsson B, Radmark O. Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75. Biochem J. 2001 Oct 15;359(Pt 2):255-63. PMID:11583571
- ↑ Li X, Liu X, Lou Z, Duan X, Wu H, Liu Y, Rao Z. Crystal structure of human coactosin-like protein at 1.9 A resolution. Protein Sci. 2004 Nov;13(11):2845-51. Epub 2004 Sep 30. PMID:15459340 doi:10.1110/ps.04937304
