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| - | [[Image:2afg.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2afg| PDB=2afg | SCENE= }} | | {{STRUCTURE_2afg| PDB=2afg | SCENE= }} |
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| - | '''2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR'''
| + | ===2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR=== |
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| - | ==Overview==
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| - | Fibroblast growth factors (FGFs) are mitogenic and chemotactic agents for a wide variety of cell types and play a primary role in the regulation of angiogenesis. Angiogenesis is involved in a variety of critical physiological events including organogenesis, wound healing, ischemic collateral circulation, and solid tumor growth. High-resolution structural information is key to understanding the mechanism of action of these growth factors. We report here the X-ray crystal structure of human acidic FGF (aFGF), with data extending to 2.0 angstroms resolution. The crystal contains four independent molecules in the asymmetric unit. Each molecule contains a single bound sulfate ion, in similar juxtapositions. The bound sulfate is stabilized through hydrogen-bond interactions with residues Asn 18, Lys 113, and Lys 118 and defines a potential heparin binding site. The hydrogen bond with the N delta 2 moiety of Asn 18 appears to be the most conserved interaction, being similar to those observed for sulfate ion bound to human basic FGF (bFGF) and similar but not identical to interactions observed for bovine aFGF with heparin analogs. Of the added solvent groups, five ordered water molecules are conserved in each of the four independent structures of human aFGF. These water molecules, located at buried positions, provide hydrogen bonding partnerships with several buried polar groups in the core of the protein. A central interior cavity exists in each of the four structures, with sizes ranging from approximately 20 to 50 angstroms3. The cavity sizes appear to be significantly smaller than that observed in the related protein interleukin-1 beta. The region comprising the high affinity FGF receptor binding site is structurally very similar to the corresponding region from human bFGF, whereas the low affinity site is structurally quite different. The results provide a structural basis for the role of the low affinity binding site in FGF receptor discrimination.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8652550}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8652550 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8652550}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Thomas, K A.]] | | [[Category: Thomas, K A.]] |
| | [[Category: Growth factor]] | | [[Category: Growth factor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:59:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:27:55 2008'' |
Revision as of 00:28, 28 July 2008
Template:STRUCTURE 2afg
2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR
Template:ABSTRACT PUBMED 8652550
About this Structure
2AFG is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1afg. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of human acidic fibroblast growth factor., Blaber M, DiSalvo J, Thomas KA, Biochemistry. 1996 Feb 20;35(7):2086-94. PMID:8652550
Page seeded by OCA on Mon Jul 28 03:27:55 2008
