PDBsum entry 1gk5

Growth factor

PDB id: 1gk5

Contents

Protein chain

49 a.a. *

* Residue conservation analysis

PDB id:

1gk5

Name:

Growth factor

Title:

Solution structure the megf/tgfalpha44-50 chimeric growth factor

Structure:

Pro-epidermal growth factor,protransforming growth factor alpha. Chain: a. Fragment: unp residues 977-1018,unp residues 83-89. Synonym: egf. Engineered: yes. Other_details: the protein is a chimera of epidermal growth factor residues 977-1018 and human transforming growth factor alpha residues 83-89,the protein is a chimera of epidermal growth factor residues

Source:

Mus musculus, homo sapiens. House mouse, human. Organism_taxid: 10090, 9606. Gene: egf, tgfa. Expressed in: komagataella pastoris. Expression_system_taxid: 4922.

NMR struc:

10 models

Authors:

S.G.Chamberlin,L.Brennan,S.M.Puddicombe,D.E.Davies,D.L.Turner

Key ref:

S.G.Chamberlin et al. (2001). Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor. Eur J Biochem, 268, 6247-6255. PubMed id: 11733021 DOI: 10.1046/j.0014-2956.2001.02581.x

Date:

08-Aug-01 Release date: 08-Aug-02

Protein chain

P01132  (EGF_MOUSE) -  Pro-epidermal growth factor from Mus musculus

Seq: 1217 a.a.

Struc: 49 a.a.*

Protein chain

P01135  (TGFA_HUMAN) -  Protransforming growth factor alpha from Homo sapiens

Seq: 160 a.a.

Struc: 49 a.a.*

* PDB and UniProt seqs differ at 33 residue positions (black crosses)

DOI no: 10.1046/j.0014-2956.2001.02581.x

Eur J Biochem 268:6247-6255 (2001)

PubMed id: 11733021

Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor.

S.G.Chamberlin, L.Brennan, S.M.Puddicombe, D.E.Davies, D.L.Turner.

ABSTRACT

The solution structure of the growth factor chimera mEGF/TGFalpha44-50 has been determined using an extended version of the dyana procedure for calculating structures from NMR data. The backbone fold and preferred orientation of the domains of the chimera are similar to those found in previous studies of EGF structures, and several H-bonds used as input constraints in those studies were found independently in the chimera. This shows that the modified activity of the chimera does not result from a major structural change. However, the improved precision of the structure presented here allows the origin of some unusual chemical shifts found in all of these compounds to be explained, as well as the results obtained from some site-specific mutants. Further studies of the properties of this chimeric growth factor should help to elucidate the mechanism(s) of hetero- and homodimerization of the c-erbB receptors.

Selected figure(s)

Figure 1.
Fig. 1 NMR Data. Top: the number of meaningful NOE-derived constraints for each residue used in the calculations. White represents intraresidual constraints ( i = 0), light grey sequential ( i = 1), grey and black represent medium ( i < 5) and long-range ( i 5) constraints. Both lower and upper volume limits are included. Bottom: average rmsd (Å) for the backbone ( ) and heavy atoms ( ) with respect to the mean structure. The superimposition was performed for residues 5–47.

Figure 2.
Fig. 2 Stereo view of the of the 10 best chimera structures, superimposed using the backbones of residues 5–47.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2001, 268, 6247-6255) copyright 2001.

Figures were selected by an automated process.