2erm: Difference between revisions
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|PDB= 2erm |SIZE=350|CAPTION= <scene name='initialview01'>2erm</scene> | |PDB= 2erm |SIZE=350|CAPTION= <scene name='initialview01'>2erm</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | |LIGAND= <scene name='pdbligand=GNS:N-SULFO-ALPHA-D-GLUCOSAMINE'>GNS</scene>, <scene name='pdbligand=IDR:L-IDURONIC+ACID'>IDR</scene>, <scene name='pdbligand=IDS:O2-SULFO-GLUCURONIC+ACID'>IDS</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NGS:N-ACETYL-D-GLUCOSAMINE-6-SULFATE+GROUP'>NGS</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FGF1, FGFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= FGF1, FGFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2erm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erm OCA], [http://www.ebi.ac.uk/pdbsum/2erm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2erm RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The 3D structure of a complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed synthetic heparin hexasaccharide has been determined by NMR spectroscopy. This hexasaccharide can substitute natural heparins in FGF-1 mitogenesis assays, in spite of not inducing any apparent dimerization of the growth factor. The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity. | The 3D structure of a complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed synthetic heparin hexasaccharide has been determined by NMR spectroscopy. This hexasaccharide can substitute natural heparins in FGF-1 mitogenesis assays, in spite of not inducing any apparent dimerization of the growth factor. The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Martin-Lomas, M.]] | [[Category: Martin-Lomas, M.]] | ||
[[Category: Nieto, P M.]] | [[Category: Nieto, P M.]] | ||
[[Category: fibroblast growth factor]] | [[Category: fibroblast growth factor]] | ||
[[Category: heparin-like hexasaccharide]] | [[Category: heparin-like hexasaccharide]] | ||
[[Category: protein-carbohydrate complex]] | [[Category: protein-carbohydrate complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:52:54 2008'' |
Revision as of 02:52, 31 March 2008
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Ligands: | , , , , | ||||||
Gene: | FGF1, FGFA (Homo sapiens) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Solution structure of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue
OverviewOverview
The 3D structure of a complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed synthetic heparin hexasaccharide has been determined by NMR spectroscopy. This hexasaccharide can substitute natural heparins in FGF-1 mitogenesis assays, in spite of not inducing any apparent dimerization of the growth factor. The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity.
About this StructureAbout this Structure
2ERM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue., Canales A, Lozano R, Lopez-Mendez B, Angulo J, Ojeda R, Nieto PM, Martin-Lomas M, Gimenez-Gallego G, Jimenez-Barbero J, FEBS J. 2006 Oct;273(20):4716-27. Epub 2006 Sep 21. PMID:16995857
Page seeded by OCA on Mon Mar 31 02:52:54 2008