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1gk5
From Proteopedia
| 1gk5, 10 NMR models () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
SOLUTION STRUCTURE THE MEGF/TGFALPHA44-50 CHIMERIC GROWTH FACTOR
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.
Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor., Chamberlin SG, Brennan L, Puddicombe SM, Davies DE, Turner DL, Eur J Biochem. 2001 Dec;268(23):6247-55. PMID:11733021
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1gk5 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA.
Reference
- Chamberlin SG, Brennan L, Puddicombe SM, Davies DE, Turner DL. Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor. Eur J Biochem. 2001 Dec;268(23):6247-55. PMID:11733021
- Puddicombe SM, Wood L, Chamberlin SG, Davies DE. The interaction of an epidermal growth factor/transforming growth factor alpha tail chimera with the human epidermal growth factor receptor reveals unexpected complexities. J Biol Chem. 1996 Nov 29;271(48):30392-7. PMID:8940002
