1T2L

Three Crystal Structures of Human Coactosin-like Protein

Summary for 1T2L

• Entry DOI: 10.2210/pdb1t2l/pdb
• Descriptor: Coactosin-like protein (2 entities in total)
• Functional Keywords: beta-sheet, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton (By similarity): Q14019
• Total number of polymer chains: 2
• Total formula weight: 31763.32

Authors

Liu, L.,Wei, Z.,Chen, Z.,Wang, Y.,Gong, W. (deposition date: 2004-04-22, release date: 2004-11-23, Last modification date: 2024-10-09)

Primary citation

Liu, L.,Wei, Z.,Wang, Y.,Wan, M.,Cheng, Z.,Gong, W.
Crystal Structure of Human Coactosin-like Protein
J.Mol.Biol., 344:317-323, 2004

PubMed Abstract: 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.

PubMed: 15522287
DOI: 10.1016/j.jmb.2004.09.036

Experimental method

X-RAY DIFFRACTION (2.8 Å)