1fmm
| |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF NFGF-1
OverviewOverview
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 StructureAbout this Structure
1FMM is a Single protein structure of sequence from Notophthalmus viridescens. Full crystallographic information is available from OCA.
ReferenceReference
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 Sun Mar 30 20:25:56 2008