1t2l
From Proteopedia
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|PDB= 1t2l |SIZE=350|CAPTION= <scene name='initialview01'>1t2l</scene>, resolution 2.8Å | |PDB= 1t2l |SIZE=350|CAPTION= <scene name='initialview01'>1t2l</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2l OCA], [http://www.ebi.ac.uk/pdbsum/1t2l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t2l RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Cardiomyopathy, dilated, 1M OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600824 600824]] | ||
==About this Structure== | ==About this Structure== | ||
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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 Sun Mar 30 23:50:23 2008'' |
Revision as of 20:50, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Three Crystal Structures of Human Coactosin-like Protein
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.
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 Sun Mar 30 23:50:23 2008
Categories: Homo sapiens | Single protein | Chen, Z. | Gong, W. | Liu, L. | Wang, Y. | Wei, Z. | Beta-sheet
