1VFQ

The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution

Summary for 1VFQ

• Entry DOI: 10.2210/pdb1vfq/pdb
• Descriptor: Coactosin-like protein (2 entities in total)
• Functional Keywords: cytoskeleton, actin-binding protein, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton (By similarity): Q14019
• Total number of polymer chains: 1
• Total formula weight: 16053.04

Authors

Li, X.,Liu, Y.,Liu, X.,Lou, Z. (deposition date: 2004-04-19, release date: 2005-01-25, Last modification date: 2023-12-27)

Primary citation

Li, X.,Liu, X.,Lou, Z.,Duan, X.,Wu, H.,Liu, Y.,Rao, Z.
Crystal structure of human coactosin-like protein at 1.9 A resolution
PROTEIN SCI., 13:2845-2851, 2004

PubMed Abstract: Human coactosin-like protein (CLP) shares high homology with coactosin, a filamentous (F)-actin binding protein, and interacts with 5LO and F-actin. As a tumor antigen, CLP is overexpressed in tumor tissue cells or cell lines, and the encoded epitopes can be recognized by cellular and humoral immune systems. To gain a better understanding of its various functions and interactions with related proteins, the crystal structure of CLP expressed in Escherichia coli has been determined to 1.9 A resolution. The structure features a central beta-sheet surrounded by helices, with two very tight hydrophobic cores on each side of the sheet. CLP belongs to the actin depolymerizing protein superfamily, and is similar to yeast cofilin and actophilin. Based on our structural analysis, we observed that CLP forms a polymer along the crystallographic b axis with the exact same repeat distance as F-actin. A model for the CLP polymer and F-actin binding has therefore been proposed.

PubMed: 15459340
DOI: 10.1110/ps.04937304

Experimental method

X-RAY DIFFRACTION (1.9 Å)