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

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

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AnimalsDimerizationEpidermal Growth FactorHydrogen BondingMagnetic Resonance SpectroscopyMiceModels, MolecularMutagenesis, Site-DirectedPeptide FragmentsProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsSolutionsTransforming Growth Factor alphaJournal Article

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S G Chamberlin, L Brennan, S M Puddicombe, D E Davies, D L Turner. 2001. Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor.. https://doi.org/10.1046/j.0014-2956.2001.02581.x

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