Three-Dimensional Structures of Acidic and Basic Fibroblast Growth Factors
Abstract
Members of the fibroblast growth factor (FGF) family of proteins stimulate the proliferation and differentiation of a variety of cell types through receptor-mediated pathways. The three-dimensional structures of two members of this family, bovine acidic FGF and human basic FGF, have been crystallographically determined. These structures contain 12 antiparallel β strands organized into a folding pattern with approximate threefold internal symmetry. Topologically equivalent folds have been previously observed for soybean trypsin inhibitor and interleukins-1β and -1α. The locations of sequences implicated in receptor and heparin binding by FGF are presented. These sites include beta-sheet strand 10, which is adjacent to the site of an extended sequence insertion in several oncogene proteins of the FGF family, and which shows sequence conservation among the FGF family and interleukin-1β.
Additional Information
© 1991 American Association for the Advancement of Science. Received 19 September 1990; accepted 21 November 1990. Supported by the Beckman Institute and the Joseph Irvine Equipment Fund. D.C.R. is an A. P. Sloan Research Fellow. Coordinates will be deposited in the Brookhaven Protein Data Bank after refinement. Current coordinates may be obtained by sending a tape to D.C.R. or by Bitnet (REES@CITRAY).Additional details
- Eprint ID
- 52453
- Resolver ID
- CaltechAUTHORS:20141208-084711342
- Caltech Beckman Institute
- Joseph Irvine Equipment Fund
- Created
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2014-12-09Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field