1VFQ

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

1VFQ の概要

• エントリーDOI: 10.2210/pdb1vfq/pdb
• 分子名称: Coactosin-like protein (2 entities in total)
• 機能のキーワード: cytoskeleton, actin-binding protein, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton (By similarity): Q14019
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16053.04

構造登録者

Li, X.,Liu, Y.,Liu, X.,Lou, Z. (登録日: 2004-04-19, 公開日: 2005-01-25, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)