1fmm

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmm OCA], [http://www.ebi.ac.uk/pdbsum/1fmm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fmm RCSB]</span>
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'''SOLUTION STRUCTURE OF NFGF-1'''
'''SOLUTION STRUCTURE OF NFGF-1'''
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[[Category: Srisailam, S.]]
[[Category: Srisailam, S.]]
[[Category: Yu, C.]]
[[Category: Yu, C.]]
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[[Category: growth factor]]
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[[Category: Growth factor]]
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[[Category: mitogen]]
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[[Category: Mitogen]]
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[[Category: triple resonance]]
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[[Category: Triple resonance]]
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[[Category: wound healing]]
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[[Category: Wound healing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:30:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:25:56 2008''
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Revision as of 13:30, 2 May 2008

Template:STRUCTURE 1fmm

SOLUTION STRUCTURE OF NFGF-1


Overview

The 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.

About this Structure

1FMM is a Single protein structure of sequence from Notophthalmus viridescens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 16:30:36 2008

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