1FMM
SOLUTION STRUCTURE OF NFGF-1
Summary for 1FMM
| Entry DOI | 10.2210/pdb1fmm/pdb |
| Descriptor | ACIDIC FIBROBLAST GROWTH FACTOR (1 entity in total) |
| Functional Keywords | growth factor, triple resonance, mitogen, wound healing, hormone-growth factor complex, hormone/growth factor |
| Biological source | Notophthalmus viridescens (eastern newt) |
| Cellular location | Secreted (By similarity): Q7SIF8 |
| Total number of polymer chains | 1 |
| Total formula weight | 15033.87 |
| Authors | Arunkumar, A.I.,Srisailam, S.,Kumar, T.K.S.,Chiu, I.M.,Yu, C. (deposition date: 2000-08-18, release date: 2001-08-18, Last modification date: 2024-05-22) |
| Primary citation | Arunkumar, A.I.,Srisailam, S.,Kumar, T.K.,Kathir, K.M.,Chi, Y.H.,Wang, H.M.,Chang, G.G.,Chiu, I.,Yu, C. Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens. J.Biol.Chem., 277:46424-46432, 2002 Cited by PubMed Abstract: 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. PubMed: 12205097DOI: 10.1074/jbc.M207814200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
