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.
==Disease==
Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]], LADD syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]]


==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: IPA]]
[[Category: fibroblast growth factor]]
[[Category: fibroblast growth factor]]
[[Category: heparin-like hexasaccharide]]
[[Category: heparin-like hexasaccharide]]
[[Category: protein-carbohydrate complex]]
[[Category: protein-carbohydrate complex]]


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Revision as of 02:52, 31 March 2008

File:2erm.jpg


PDB ID 2erm

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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

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