title: Crystal structure of the tenth type III cell adhesion module of human fibronectin.
abstract: The crystal structure of the cell adhesion module of fibronectin (FNIII10) has been determined at 1.8 A resolution. A recombinant fragment corresponding to the tenth type III module of human fibronectin was crystallized in space group P2(1) with a = 30.7, b = 35.1 and c = 37.7 A and beta = 107 degrees. The structure was determined by molecular replacement and refined by least squares methods. The crystallographic R-factor for the final model of the 91 amino acid module plus 56 solvent atoms is 0.18 for 10 to 1.8 A data. The module consists of two layers of beta-sheet, one with three antiparallel strands and the other with four antiparallel strands. The beta-sheets enclose a hydrophobic core of 24 amino acid side-chains. The module contains the RGD cell recognition sequence in a flexible loop connecting two beta-strands. The tertiary structure of the FNIII10 module has been used to develop a structure-based sequence alignment of 17 type III modules in fibronectin based on the striking conservation of homologous hydrophobic residues. A similar pattern of homologous alternating hydrophobic residues is also evident in a comparison of type III modules in proteins unrelated to fibronectin such as cytokine receptors and muscle proteins.
authors.affiliation: Cancer Research Center, La Jolla Cancer Research Foundation, CA 92037.
authors.forename: C D
authors.initials: CD
authors.lastname: Dickinson
authors.forename: B
authors.initials: B
authors.lastname: Veerapandian
authors.forename: X P
authors.initials: XP
authors.lastname: Dai
authors.forename: R C
authors.initials: RC
authors.lastname: Hamlin
authors.forename: N H
authors.initials: NH
authors.lastname: Xuong
authors.forename: E
authors.initials: E
authors.lastname: Ruoslahti
authors.forename: K R
authors.initials: KR
authors.lastname: Ely
mesh_terms: D000595:Amino Acid Sequence; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000235:genetics; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D005353:Fibronectins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D012997:Solvents
chemical_list: D015815:Cell Adhesion Molecules; D005353:Fibronectins; D011993:Recombinant Fusion Proteins; D012997:Solvents