PDBsum entry 1vfq

Protein binding

PDB id: 1vfq

Contents

Protein chain

132 a.a. *

Waters ×110

* Residue conservation analysis

PDB id:

1vfq

Name:

Protein binding

Title:

The crystal structure of human coactosin-like protein at 1.9 a resolution

Structure:

Coactosin-like protein. Chain: a. Synonym: clp. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å R-factor: 0.166 R-free: 0.218

Authors:

X.Li,Y.Liu,X.Liu,Z.Lou

Key ref:

X.Li et al. (2004). Crystal structure of human coactosin-like protein at 1.9 A resolution. Protein Sci, 13, 2845-2851. PubMed id: 15459340 DOI: 10.1110/ps.04937304

Date:

19-Apr-04 Release date: 25-Jan-05

Protein chain

Q14019  (COTL1_HUMAN) -  Coactosin-like protein from Homo sapiens

Seq: 142 a.a.

Struc: 132 a.a.

DOI no: 10.1110/ps.04937304

Protein Sci 13:2845-2851 (2004)

PubMed id: 15459340

Crystal structure of human coactosin-like protein at 1.9 A resolution.

X.Li, X.Liu, Z.Lou, X.Duan, H.Wu, Y.Liu, Z.Rao.

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.

Selected figure(s)

Figure 3.
Figure 3. Comparison of CLP structure with actophorin and yeast cofilin. (A) Stereo view of CLP (red) superimposed with cofilin (yellow) and actophorin (purple). The figure was prepared with MOLSCRIPT. (B) Comparison of the CLP molecular surface charge distribution with those of cofilin and actophorin. The positive charges are shown in the first row; the negative, which is the opposite sides of the positive, are shown in the second row. The surface of CLP is more positively charged in the N-terminal and 4- 5 loop regions. This figure was prepared with SPDBV (Guex and Peitsch 1997).

Figure 5.
Figure 5. A model for CLP polymer binding with F-actin and other proteins. (A) CLP polymer and F-actin have the same repeating distance. The morphologies of the two polymers match each other very well. Its long flexible C-terminal arm may help CLP binding other molecules. (B) A model for CLP polymer binding with F-actin. (C) CLP-F-actin copolymer binding with other proteins (red). The F-actin diagram is provided by Amy McGough (Baylor College of Medicine, Houston, TX). The models in B and C were prepared with Photoshop, and the charged surface model and the CPK (red) model were prepared with SPDBV and MOLSCRIPT, respectively.

The above figures are reprinted by permission from the Protein Society: Protein Sci (2004, 13, 2845-2851) copyright 2004.

Figures were selected by an automated process.