1FNA

CRYSTAL STRUCTURE OF THE TENTH TYPE III CELL ADHESION MODULE OF HUMAN FIBRONECTIN

Summary for 1FNA

• Entry DOI: 10.2210/pdb1fna/pdb
• Descriptor: FIBRONECTIN CELL-ADHESION MODULE TYPE III-10 (1 entity in total)
• Functional Keywords: cell adhesion protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P02751
• Total number of polymer chains: 1
• Total formula weight: 9691.79

Authors

Dickinson, C.D.,Veerapandian, B.,Ely, K.R. (deposition date: 1994-01-11, release date: 1994-04-30, Last modification date: 2024-02-07)

Primary citation

Dickinson, C.D.,Veerapandian, B.,Dai, X.P.,Hamlin, R.C.,Xuong, N.H.,Ruoslahti, E.,Ely, K.R.
Crystal structure of the tenth type III cell adhesion module of human fibronectin.
J.Mol.Biol., 236:1079-1092, 1994

PubMed 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.

PubMed: 8120888
DOI: 10.1016/0022-2836(94)90013-2

Experimental method

X-RAY DIFFRACTION (1.8 Å)