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2afg

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Revision as of 12:01, 10 September 2015

2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR

Structural highlights

2afg is a 4 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 1afg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[FGF1_HUMAN] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ornitz DM, Xu J, Colvin JS, McEwen DG, MacArthur CA, Coulier F, Gao G, Goldfarb M. Receptor specificity of the fibroblast growth factor family. J Biol Chem. 1996 Jun 21;271(25):15292-7. PMID:8663044
↑ Zhang X, Ibrahimi OA, Olsen SK, Umemori H, Mohammadi M, Ornitz DM. Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family. J Biol Chem. 2006 Jun 9;281(23):15694-700. Epub 2006 Apr 4. PMID:16597617 doi:10.1074/jbc.M601252200
↑ Fernandez IS, Cuevas P, Angulo J, Lopez-Navajas P, Canales-Mayordomo A, Gonzalez-Corrochano R, Lozano RM, Valverde S, Jimenez-Barbero J, Romero A, Gimenez-Gallego G. Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors. J Biol Chem. 2010 Apr 9;285(15):11714-29. Epub 2010 Feb 9. PMID:20145243 doi:10.1074/jbc.M109.064618
↑ Blaber M, DiSalvo J, Thomas KA. X-ray crystal structure of human acidic fibroblast growth factor. Biochemistry. 1996 Feb 20;35(7):2086-94. PMID:8652550 doi:http://dx.doi.org/10.1021/bi9521755

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2afg"

Categories: Human | Blaber, M | Disalvo, J | Thomas, K A | Growth factor

@@ Line 2: / Line 2: @@
 <StructureSection load='2afg' size='340' side='right' caption='[[2afg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2afg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1afg 1afg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AFG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2afg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1afg 1afg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AFG FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2afg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2afg RCSB], [http://www.ebi.ac.uk/pdbsum/2afg PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2afg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afg OCA], [http://pdbe.org/2afg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2afg RCSB], [http://www.ebi.ac.uk/pdbsum/2afg PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2afg" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Blaber, M]]
 [[Category: Disalvo, J]]
 [[Category: Thomas, K A]]
 [[Category: Growth factor]]

2afg

From Proteopedia

Revision as of 12:01, 10 September 2015

2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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