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Title: Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1

Abstract

The radixin FERM domain has been crystallized in complex with CD43 and PSGL-1 peptides. Diffraction data sets were collected from the complexes to 2.9 and 2.8 Å resolution, respectively. Radixin is a member of the ERM proteins that cross-link plasma membranes and actin filaments. The FERM domains located in the N-terminal regions of ERM proteins are responsible for membrane association through direct interaction with the cytoplasmic tails of integral membrane proteins. Here, crystals of the radixin FERM domain bound to the cytoplasmic peptides of two adhesion molecules, CD43 and PSGL-1, have been obtained. Crystals of the radixin FERM domain bound to CD43 belong to space group P4{sub 3}22, with unit-cell parameters a = b = 68.72, c = 201.39 Å, and contain one complex in the crystallographic asymmetric unit. Crystals of the radixin FERM domain bound to PSGL-1 belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 80.74, b = 85.73, c = 117.75 Å, and contain two complexes in the crystallographic asymmetric unit. Intensity data sets were collected to a resolution of 2.9 Å for the FERM–CD43 complex and 2.8 Å for the FERM–PSGL-1 complex.

Authors:
; ; ;  [1];  [1];  [2]
  1. Structural Biology Laboratory, Nara Institute of Science and Technology, Keihanna Science City, Nara 630-0192 (Japan)
  2. (Japan)
Publication Date:
OSTI Identifier:
22360249
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 1; Other Information: PMCID: PMC2330108; PMID: 17183174; PUBLISHER-ID: fw5117; OAI: oai:pubmedcentral.nih.gov:2330108; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ADHESION; CRYSTALS; DIFFRACTION; INTERACTIONS; MEMBRANES; MOLECULES; PLASMA; RESOLUTION; SPACE GROUPS

Citation Formats

Takai, Yumiko, Kitano, Ken, Terawaki, Shin-ichi, Maesaki, Ryoko, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, and CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192. Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309106054145.
Takai, Yumiko, Kitano, Ken, Terawaki, Shin-ichi, Maesaki, Ryoko, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, & CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192. Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1. United Kingdom. doi:10.1107/S1744309106054145.
Takai, Yumiko, Kitano, Ken, Terawaki, Shin-ichi, Maesaki, Ryoko, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, and CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192. Mon . "Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1". United Kingdom. doi:10.1107/S1744309106054145.
@article{osti_22360249,
title = {Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1},
author = {Takai, Yumiko and Kitano, Ken and Terawaki, Shin-ichi and Maesaki, Ryoko and Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp and CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192},
abstractNote = {The radixin FERM domain has been crystallized in complex with CD43 and PSGL-1 peptides. Diffraction data sets were collected from the complexes to 2.9 and 2.8 Å resolution, respectively. Radixin is a member of the ERM proteins that cross-link plasma membranes and actin filaments. The FERM domains located in the N-terminal regions of ERM proteins are responsible for membrane association through direct interaction with the cytoplasmic tails of integral membrane proteins. Here, crystals of the radixin FERM domain bound to the cytoplasmic peptides of two adhesion molecules, CD43 and PSGL-1, have been obtained. Crystals of the radixin FERM domain bound to CD43 belong to space group P4{sub 3}22, with unit-cell parameters a = b = 68.72, c = 201.39 Å, and contain one complex in the crystallographic asymmetric unit. Crystals of the radixin FERM domain bound to PSGL-1 belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 80.74, b = 85.73, c = 117.75 Å, and contain two complexes in the crystallographic asymmetric unit. Intensity data sets were collected to a resolution of 2.9 Å for the FERM–CD43 complex and 2.8 Å for the FERM–PSGL-1 complex.},
doi = {10.1107/S1744309106054145},
journal = {Acta Crystallographica. Section F},
number = Pt 1,
volume = 63,
place = {United Kingdom},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}