Three-dimensional structures of acidic and basic fibroblast growth factors
| Autor: | Arthur J. Chirino, Xiaotian Zhu, H. Komiya, Salem Faham, Tsutomu Arakawa, Douglas C. Rees, Gary M. Fox, Barbara T. Hsu |
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| Rok vydání: | 1991 |
| Předmět: |
Oncogene Proteins
Chemical Phenomena Protein Conformation medicine.medical_treatment Molecular Sequence Data Beta sheet Biology Fibroblast growth factor Antiparallel (biochemistry) Protein structure X-Ray Diffraction Sequence Homology Nucleic Acid medicine Animals Humans Amino Acid Sequence Peptide sequence Multidisciplinary Kunitz STI protease inhibitor Molecular Structure Chemistry Physical Heparin Growth factor Recombinant Proteins Biochemistry Fibroblast Growth Factor 1 Cattle Fibroblast Growth Factor 2 Crystallization Interleukin-1 |
| Zdroj: | Science (New York, N.Y.). 251(4989) |
| ISSN: | 0036-8075 |
| Popis: | 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 beta strands organized into a folding pattern with approximate threefold internal symmetry. Topologically equivalent folds have been previously observed for soybean trypsin inhibitor and interleukins-1 beta and -1 alpha. 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-1 beta. |
| Databáze: | OpenAIRE |
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