2erm

<StructureSection load='2erm' size='340' side='right' caption='[[2erm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2erm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNS:N-SULFO-ALPHA-D-GLUCOSAMINE'>GNS</scene>, <scene name='pdbligand=IDR:L-IDURONIC+ACID'>IDR</scene>, <scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NGY:2-(ACETYLAMINO)-2-DEOXY-6-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>NGY</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=2erm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erm OCA], [http://pdbe.org/2erm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2erm RCSB], [http://www.ebi.ac.uk/pdbsum/2erm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2erm ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/FGF1_HUMAN 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.<ref>PMID:8663044</ref> <ref>PMID:16597617</ref> <ref>PMID:20145243</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:16995857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2erm" style="background-color:#fffaf0;"></div>

*[[Fibroblast growth factor|Fibroblast growth factor]]

[[Category: Human]]

[[Category: Canales, A]]

[[Category: Gimenez-Gallego, G]]

[[Category: Jimenez-Barbero, J]]

[[Category: Lozano, R]]

[[Category: Martin-Lomas, M]]

[[Category: Nieto, P M]]

[[Category: Protein-carbohydrate complex]]