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Three-Dimensional Structures of Acidic and Basic Fibroblast Growth Factors

Zhu, X. and Komiya, H. and Chirino, A. and Faham, S. and Fox, G. M. and Arakawa, T. and Hsu, B. T. and Rees, D. C. (1991) Three-Dimensional Structures of Acidic and Basic Fibroblast Growth Factors. Science, 251 (4989). pp. 90-93. ISSN 0036-8075. doi:10.1126/science.1702556.

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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.

Item Type:Article
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Rees, D. C.0000-0003-4073-1185
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).
Funding AgencyGrant Number
Caltech Beckman InstituteUNSPECIFIED
Joseph Irvine Equipment FundUNSPECIFIED
Issue or Number:4989
Record Number:CaltechAUTHORS:20141208-084711342
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Official Citation:Three-dimensional structures of acidic and basic fibroblast growth factors X Zhu, H Komiya, A Chirino, S Faham, GM Fox, T Arakawa, BT Hsu, and DC Rees Science 4 January 1991: 251 (4989), 90-93. [DOI:10.1126/science.1702556]
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52453
Deposited By: Tony Diaz
Deposited On:09 Dec 2014 22:28
Last Modified:10 Nov 2021 19:41

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