Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44.
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.
Mori
Tomoyuki
T
Structural Biology Laboratory, Nara Institute of Science and Technology, Keihanna Science City, Nara 630-0192, Japan.
Kitano
Ken
K
Terawaki
Shin-ichi
S
Maesaki
Ryoko
R
Hakoshima
Toshio
T
D000818:Animals; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D003593:Cytoplasm / Q000737:chemistry / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism*; D018960:Hyaluronan Receptors / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary
D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D018960:Hyaluronan Receptors; D008565:Membrane Proteins; C071776:radixin