Cat. No.

CBCRY15

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

GeneID

23406

Chromosome  Location

16q24.1

Function

actin binding; protein binding

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