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Product Summary | |
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Name | COTL1 Protein Crystal Download Datasheet |
Background | |
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Background | 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. 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. |
Molecular Description | |
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Protein Classification | protein binding |
Structure Weight | 31763.60 Da |
Polymer | 1 |
Molecule | Coactosin-like protein |
Chain Length | 145 amino acids |
Crystal Description | |
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PDB ID | 1T2L |
MMDB ID | 30298 |
Source | E.coli |
Method | X-Ray Diffraction |
Resolution | 2.8 Å |
Gene Information | |
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Gene Name | COTL1 |
Synonyms | CLP; FLJ43657; MGC19733; coactosin-like 1; coactosin-like 1 (Dictyostelium) |
UniProt ID | Q14019 |
Gene ID | 23406 |
Chromosome Location | 16q24.1 |
Function | actin binding; protein binding |
Reference | |
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Reference | Liu, L., Wei, Z., Wang, Y., Wan, M., Cheng, Z., Gong, W. (2004) Crystal Structure of Human Coactosin-like Protein J.Mol.Biol. 344: 317-323 |