title: Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1.
abstract: 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(3)22, with unit-cell parameters a = b = 68.72, c = 201.39 A, and contain one complex in the crystallographic asymmetric unit. Crystals of the radixin FERM domain bound to PSGL-1 belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 80.74, b = 85.73, c = 117.75 A, and contain two complexes in the crystallographic asymmetric unit. Intensity data sets were collected to a resolution of 2.9 A for the FERM-CD43 complex and 2.8 A for the FERM-PSGL-1 complex.
authors.affiliation: Structural Biology Laboratory, Nara Institute of Science and Technology, Keihanna Science City, Nara 630-0192, Japan.
authors.forename: Yumiko
authors.initials: Y
authors.lastname: Takai
authors.forename: Ken
authors.initials: K
authors.lastname: Kitano
authors.forename: Shin-ichi
authors.initials: S
authors.lastname: Terawaki
authors.forename: Ryoko
authors.initials: R
authors.lastname: Maesaki
authors.forename: Toshio
authors.initials: T
authors.lastname: Hakoshima
mesh_terms: D000818:Animals; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism; D016764:Cell Polarity; D018360:Crystallography, X-Ray / Q000379:methods; D003593:Cytoplasm / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000378:metabolism; D051917:Leukosialin / Q000737:chemistry* / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D051379:Mice; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary
chemical_list: D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D051917:Leukosialin; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C084882:P-selectin ligand protein; C071776:radixin