Structure of rat acidic fibroblast growth factor at 1.4 Å resolution

Journal Article · Thu Feb 01 00:00:00 EST 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107003144· OSTI ID:22360259

Kulahin, Nikolaj ^[1]; Kiselyov, Vladislav ^[1]; Kochoyan, Arthur ^[1]; Kristensen, Ole; Kastrup, Jette Sandholm ^[2]; Berezin, Vladimir; Bock, Elisabeth ^[1]; Gajhede, Michael ^[2]

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1. Protein Laboratory, Institute of Molecular Pathology, Panum Institute, Blegdamsvej 3C, DK-2200 Copenhagen (Denmark)
2. Biostructural Research, Department of Medicinal Chemistry, Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen (Denmark)

The structure of rat acidic fibroblast growth factor was determined and compared with those of human, bovine and newt origin. The rat and human structures were found to be very similar. Fibroblast growth factors (FGFs) constitute a family of 22 structurally related heparin-binding polypeptides that are involved in the regulation of cell growth, survival, differentiation and migration. Here, a 1.4 Å resolution X-ray structure of rat FGF1 is presented. Two molecules are present in the asymmetric unit of the crystal and they coordinate a total of five sulfate ions. The structures of human, bovine and newt FGF1 have been published previously. Human and rat FGF1 are found to have very similar structures.

• OSTI ID: 22360259
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 2; Other Information: PMCID: PMC2330123; PMID: 17277441; PUBLISHER-ID: fw5120; OAI: oai:pubmedcentral.nih.gov:2330123; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CATTLE
CRYSTALS
FIBROBLASTS
MIGRATION
MOLECULES
ORIGIN
RATS
RESOLUTION
SULFATES