TAILIEUCHUNG - Báo cáo Y học: Solution structure of the mEGF/TGFa44250 chimeric growth factor

The solution structure of the growth factor chimera mEGF/ TGFa44250 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 Epidermal growth factor (EGF) [1,2] and transforming growth factor alpha (TGFa). | Eur. J. Biochem. 268 6247-6255 2001 FEBS 2001 Solution structure of the mEGF TGFa44_50 chimeric growth factor Stephen G. Chamberlin1 Lorraine Brennan2 t Sarah M. Puddicombe1 Donna E. Davies1 and David L. Turner2 1 Cancer Research Campaign Medical Oncology Unit Southampton General Hospital Southampton UK department of Chemistry University of Southampton Highfield Southampton UK The solution structure of the growth factor chimera mEGF TGFa44_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 sitespecific 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. Keywords NMR EGF structure growth factor INDYANA simulated annealing. Epidermal growth factor EGF 1 2 and transforming growth factor alpha TGFa 3 are members of a family that also includes heparin-binding EGF-like growth factor 4 amphiregulin 5 betacellulin 6 epiregulin 7 and the heregulins 8 9 . These growth factors play important roles in cell growth and differentiation 10 through their interaction with members of the c-erbB family of receptor tyrosine kinases 11 . They are characterized by a three-looped EGF motif imposed by three highly conserved intramolecular disulfide bonds as well as by the presence of a number of other conserved residues that have been shown to be required for biological .

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