1t2l
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Human coactosin-like protein is an actin filament binding protein but does | + | Human coactosin-like protein is an actin filament binding protein but does not bind to globular actin. It associates with 5-Lipoxygenase both in vivo and in vitro, playing important roles in modulating the activities of actin and 5-Lipoxygenase. Coactosin counteracts the capping activity of capping protein which inhibits the actin polymerization. We determined the crystal structures of human coactosin-like protein by multi-wavelength anomalous dispersion method. The structure showed a high level of similarity to ADF-H domain, although their amino acid sequences share low degree of homology. A few conserved hydrophobic residues that may contribute to the folding were identified. This structure suggests coactosin-like protein bind to F-actin in a different way from ADF/Cofilin family. Combined with the information from previous mutagenesis studies, the binding sites for F-actin and 5-Lipoxygenase were analyzed, respectively. These two sites are quite close, which might prevent F-actin and 5-Lipoxygenase from binding to coactosin simultaneously. |
==Disease== | ==Disease== | ||
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[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:15 2008'' |
Revision as of 13:09, 21 February 2008
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Three Crystal Structures of Human Coactosin-like Protein
Contents |
Overview
Human coactosin-like protein is an actin filament binding protein but does not bind to globular actin. It associates with 5-Lipoxygenase both in vivo and in vitro, playing important roles in modulating the activities of actin and 5-Lipoxygenase. Coactosin counteracts the capping activity of capping protein which inhibits the actin polymerization. We determined the crystal structures of human coactosin-like protein by multi-wavelength anomalous dispersion method. The structure showed a high level of similarity to ADF-H domain, although their amino acid sequences share low degree of homology. A few conserved hydrophobic residues that may contribute to the folding were identified. This structure suggests coactosin-like protein bind to F-actin in a different way from ADF/Cofilin family. Combined with the information from previous mutagenesis studies, the binding sites for F-actin and 5-Lipoxygenase were analyzed, respectively. These two sites are quite close, which might prevent F-actin and 5-Lipoxygenase from binding to coactosin simultaneously.
Disease
Known disease associated with this structure: Cardiomyopathy, dilated, 1M OMIM:[600824]
About this Structure
1T2L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human coactosin-like protein., Liu L, Wei Z, Wang Y, Wan M, Cheng Z, Gong W, J Mol Biol. 2004 Nov 19;344(2):317-23. PMID:15522287
Page seeded by OCA on Thu Feb 21 15:09:15 2008
Categories: Homo sapiens | Single protein | Chen, Z. | Gong, W. | Liu, L. | Wang, Y. | Wei, Z. | Beta-sheet
