1fmm: Difference between revisions
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==SOLUTION STRUCTURE OF NFGF-1== | ==SOLUTION STRUCTURE OF NFGF-1== | ||
<StructureSection load='1fmm' size='340' side='right'caption='[[1fmm | <StructureSection load='1fmm' size='340' side='right'caption='[[1fmm]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1fmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Notophthalmus_viridescens Notophthalmus viridescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMM FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmm OCA], [https://pdbe.org/1fmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmm RCSB], [https://www.ebi.ac.uk/pdbsum/1fmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmm ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmm OCA], [https://pdbe.org/1fmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmm RCSB], [https://www.ebi.ac.uk/pdbsum/1fmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmm ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FGF1_NOTVI FGF1_NOTVI] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arunkumar | [[Category: Notophthalmus viridescens]] | ||
[[Category: Chiu | [[Category: Arunkumar AI]] | ||
[[Category: Kumar | [[Category: Chiu IM]] | ||
[[Category: Srisailam | [[Category: Kumar TKS]] | ||
[[Category: Yu | [[Category: Srisailam S]] | ||
[[Category: Yu C]] | |||
Latest revision as of 11:29, 22 May 2024
SOLUTION STRUCTURE OF NFGF-1SOLUTION STRUCTURE OF NFGF-1
Structural highlights
FunctionFGF1_NOTVI Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro (By similarity). 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 PubMedThe three-dimensional solution structure of an acidic fibroblast growth factor (nFGF-1) from the newt (Notophthalmus viridescens) is determined using multidimensional NMR techniques. Complete assignment of all the atoms ((1)H, (15)N, and (13)C) has been achieved using a variety of triple resonance experiments. 50 structures were calculated using hybrid distance geometry-dynamical simulated annealing technique with a total of 1359 constraints. The atomic root mean square distribution for the backbone atoms in the structured region is 0.60 A. The secondary structural elements include 12 beta-strands arranged antiparallely into a beta-barrel structure. The protein (nFGF-1) exists in a monomeric state upon binding to the ligand, sucrose octa sulfate (SOS), in a stoichiometric ratio of 1:1. The SOS binding site consists of a dense cluster of positively charged residues located at the C-terminal end of the molecule. The conformational stabilities of nFGF-1 and its structural and functional homologue from the human source (hFGF-1) are drastically different. The differential stabilities of nFGF-1 and hFGF-1 are attributed to the differences in the number of hydrogen bonds and the presence of solvent inaccessible cavities in the two proteins. Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens.,Arunkumar AI, Srisailam S, Kumar TK, Kathir KM, Chi YH, Wang HM, Chang GG, Chiu I, Yu C J Biol Chem. 2002 Nov 29;277(48):46424-32. Epub 2002 Aug 29. PMID:12205097[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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