skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Crystal structure of the N-terminal SH3 domain of mouse {beta}PIX, p21-activated kinase-interacting exchange factor

Abstract

The mouse {beta}PIX-SH3 domain, residues 8-63 of P21-activated kinase interacting exchange factor, has been characterized by X-ray diffraction. Crystals belonging to space group P3{sub 2}21 diffracted to 2.0 A and the structure was phased by the single-wavelength anomalous diffraction method. The domain is a compact {beta}-barrel with an overall conformation similar to the general SH3 structure. The X-ray structure shows mouse {beta}PIX-SH3 domain binding the way in which the {beta}PIX characteristic amino acids do so for an unconventional ligand binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by mouse {beta}PIX-SH3 domain. Comparison with another SH3/peptide complex shows that the recognition mode of the mouse {beta}PIX-SH3 domain should be very similar to the RXXK ligand binding mode. The unique large and planar hydrophobic pocket may contribute to the promiscuity of {beta}PIX-SH3 domain resulting in its multiple biological functions.

Authors:
 [1];  [1];  [1];  [1];  [1];  [2];  [1];  [3]
  1. Laboratory of Structural Biology, Tsinghua University, Beijing 100084 (China)
  2. Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080 (China)
  3. Laboratory of Structural Biology, Tsinghua University, Beijing 100084 (China) and National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101 (China)
Publication Date:
OSTI Identifier:
20795865
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 339; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2005.10.212; PII: S0006-291X(05)02447-2; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACIDS; BIOLOGICAL FUNCTIONS; CRYSTALS; LIGANDS; MICE; PEPTIDES; TRIGONAL LATTICES; X-RAY DIFFRACTION

Citation Formats

Xiaofeng, Li, Xueqi, Liu, National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101, Fei, Sun, Jia, Gao, Hongwei, Zhou, Gao, George F, Bartlam, Mark, National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101, and Zihe, Rao. Crystal structure of the N-terminal SH3 domain of mouse {beta}PIX, p21-activated kinase-interacting exchange factor. United States: N. p., 2006. Web. doi:10.1016/J.BBRC.2005.1.
Xiaofeng, Li, Xueqi, Liu, National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101, Fei, Sun, Jia, Gao, Hongwei, Zhou, Gao, George F, Bartlam, Mark, National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101, & Zihe, Rao. Crystal structure of the N-terminal SH3 domain of mouse {beta}PIX, p21-activated kinase-interacting exchange factor. United States. https://doi.org/10.1016/J.BBRC.2005.1
Xiaofeng, Li, Xueqi, Liu, National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101, Fei, Sun, Jia, Gao, Hongwei, Zhou, Gao, George F, Bartlam, Mark, National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101, and Zihe, Rao. 2006. "Crystal structure of the N-terminal SH3 domain of mouse {beta}PIX, p21-activated kinase-interacting exchange factor". United States. https://doi.org/10.1016/J.BBRC.2005.1.
@article{osti_20795865,
title = {Crystal structure of the N-terminal SH3 domain of mouse {beta}PIX, p21-activated kinase-interacting exchange factor},
author = {Xiaofeng, Li and Xueqi, Liu and National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101 and Fei, Sun and Jia, Gao and Hongwei, Zhou and Gao, George F and Bartlam, Mark and National Laboratory of Biomacromolecules, Institutes of Biophysics, Chinese Academy of Sciences, Beijing 100101 and Zihe, Rao},
abstractNote = {The mouse {beta}PIX-SH3 domain, residues 8-63 of P21-activated kinase interacting exchange factor, has been characterized by X-ray diffraction. Crystals belonging to space group P3{sub 2}21 diffracted to 2.0 A and the structure was phased by the single-wavelength anomalous diffraction method. The domain is a compact {beta}-barrel with an overall conformation similar to the general SH3 structure. The X-ray structure shows mouse {beta}PIX-SH3 domain binding the way in which the {beta}PIX characteristic amino acids do so for an unconventional ligand binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by mouse {beta}PIX-SH3 domain. Comparison with another SH3/peptide complex shows that the recognition mode of the mouse {beta}PIX-SH3 domain should be very similar to the RXXK ligand binding mode. The unique large and planar hydrophobic pocket may contribute to the promiscuity of {beta}PIX-SH3 domain resulting in its multiple biological functions.},
doi = {10.1016/J.BBRC.2005.1},
url = {https://www.osti.gov/biblio/20795865}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 1,
volume = 339,
place = {United States},
year = {Fri Jan 06 00:00:00 EST 2006},
month = {Fri Jan 06 00:00:00 EST 2006}
}