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COTL1 Protein Crystal

(CBCRY15)  Download Datasheet
Background
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
Protein Classification
protein binding
Structure Weight
31763.60 Da
Polymer
1
Molecule
Coactosin-like protein
Chain Length
145 amino acids
Crystal Description
PDB ID
1T2L
MMDB ID
30298
Source
E.coli
Method
X-Ray Diffraction
Resolution
2.8 Å
Gene Information
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
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