Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt 10):844-7. doi: 10.1107/S1744309107041152. Epub 2007 Sep 19.

Abstract

CD44 is an important adhesion molecule that specifically binds hyaluronic acid and regulates cell-cell and cell-matrix interactions. Increasing evidence has indicated that CD44 is assembled in a regulated manner into the membrane-cytoskeletal junction, a process that is mediated by ERM (ezrin/radixin/moesin) proteins. Crystals of a complex between the radixin FERM domain and the C-terminal cytoplasmic region of CD44 have been obtained. The crystal of the radixin FERM domain bound to the CD44 cytoplasmic tail peptide belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 62.70, b = 66.18, c = 86.22 A, and contain one complex in the crystallographic asymmetric unit. An intensity data set was collected to a resolution of 2.1 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism*
  • Crystallography, X-Ray
  • Cytoplasm / chemistry
  • Cytoplasm / metabolism*
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / metabolism*
  • Hyaluronan Receptors / chemistry
  • Hyaluronan Receptors / metabolism
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Mice
  • Protein Binding / physiology
  • Protein Structure, Tertiary

Substances

  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • Hyaluronan Receptors
  • Membrane Proteins
  • radixin