1g82

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spinqualitylabelsall models 1g82, resolution 2.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF FIBROBLAST GROWTH FACTOR 9

Overview

Fibroblast growth factors (FGFs) constitute a family of at least 20, structurally related heparin-binding polypeptides active in regulating, cell growth, survival, differentiation and migration. FGF9, originally, discovered as a glia-activating factor, shares 30% sequence identity with, other FGFs and has a unique spectrum of target-cell specificity. FGF9, crystallized in the tetragonal space group I4(1), with unit-cell, parameters a = b = 151.9, c = 117.2 A. The structure of the glycosylated, protein has been refined to an R value of 21.0% with R(free) = 24.8%) at, 2.6 A resolution. The four molecules in the asymmetric unit are arranged, in two non-crystallographic dimers, with the dimer interface composed, partly of residues from N- and C-terminal extensions from the FGF core, structure. Most of the receptor-binding residues identified in FGF1- and, FGF2-receptor complexes are buried in the dimer interface, with the, beta8-beta9 loop stabilized in a particular conformation by an, intramolecular hydrogen-bonding network. The potential heparin-binding, sites are in a pattern distinct from FGF1 and FGF2. The carbohydrate, moiety attached at Asn79 has no structural influence.

About this Structure

1G82 is a Single protein structure of sequence from Homo sapiens with NAG and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:11223514

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