PDBsum entry: 1fmm

Hormone/growth factor

PDB id: 1fmm

Contents

Protein chain

132 a.a. *

* Residue conservation analysis

PDB id:

1fmm

Name:

Hormone/growth factor

Title:

Solution structure of nfgf-1

Structure:

Acidic fibroblast growth factor. Chain: s. Synonym: nfgf-1. Engineered: yes

Source:

Notophthalmus viridescens. Eastern newt. Organism_taxid: 8316. Cell: fibroblast. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

A.I.Arunkumar,S.Srisailam,T.K.S.Kumar,I.M.Chiu,C.Yu

Key ref:

A.I.Arunkumar et al. (2002). Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens. J Biol Chem, 277, 46424-46432. PubMed id: 12205097 DOI: 10.1074/jbc.M207814200

Date:

18-Aug-00 Release date: 18-Aug-01

Protein chain

Q7SIF8  (FGF1_NOTVI) -  Heparin-binding growth factor 1 (Fragment)

Seq: 132 a.a.

Struc: 132 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: multicellular organismal development (4 terms)
• Biochemical function: growth factor activity (2 terms)

DOI no: 10.1074/jbc.M207814200

J Biol Chem 277:46424-46432 (2002)

PubMed id: 12205097

Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens.

A.I.Arunkumar, S.Srisailam, T.K.Kumar, K.M.Kathir, Y.H.Chi, H.M.Wang, G.G.Chang, I.Chiu, C.Yu.

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.

Selected figure(s)

Figure 5.
Fig. 5. Intermolecular NOEs characterizing the interaction of nFGF-1 and SOS. Most of the NOEs represent interactions between the side chains of charged resides located at the C-terminal end of the molecule of nFGF-1 and the protons in the six-membered pyranose ring of SOS .

Figure 6.
Fig. 6. Ensemble of structures of nFGF-1 in complex with SOS. SOS interacts (indicated in yellow) with the dense cluster of positively charged residues located at the C-terminal end (blue) of the nFGF-1 molecule. The protein mostly interacts with the pyranose ring of the SOS molecule.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 46424-46432) copyright 2002.

Figures were selected by an automated process.