1GK5

Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor

Summary for 1GK5

• Entry DOI: 10.2210/pdb1gk5/pdb
• NMR Information: BMRB: 5120
• Descriptor: Pro-epidermal growth factor,Protransforming growth factor alpha (1 entity in total)
• Functional Keywords: growth factor, egf growth factor, chimeric
• Biological source: Mus musculus (House Mouse); More
• Cellular location: Transforming growth factor alpha: Secreted, extracellular space. Protransforming growth factor alpha: Cell membrane; Single-pass type I membrane protein: P01135
• Total number of polymer chains: 1
• Total formula weight: 5257.78

Authors

Chamberlin, S.G.,Brennan, L.,Puddicombe, S.M.,Davies, D.E.,Turner, D.L. (deposition date: 2001-08-08, release date: 2002-08-08, Last modification date: 2024-11-13)

Primary citation

Chamberlin, S.,Brennan, L.,Puddicombe, S.,Davies, D.,Turner, D.
Solution Structure of the Megf/Tgfalpha44-50 Chimeric Growth Factor.
Eur.J.Biochem., 268:6247-, 2001

PubMed 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.

PubMed: 11733021
DOI: 10.1046/J.0014-2956.2001.02581.X

Experimental method

SOLUTION NMR