Solution structure of the mEGF/TGF ?(44-50) chimeric growth factor
Solution structure of the mEGF/TGF ?(44-50) chimeric growth factor
The solution structure of the growth factor chimera mEGF/TGF ?(44-50) 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.
nmr, egf structure, growth factor, indyana, simulated annealing, relaxation matrix approach, factor receptor, factor-? protein structures, tgf-?, biological macromolecules, signal-transduction, chemical-shift, binding
6247-6255
Chamberlin, Stephen G.
ecb947dd-c59e-4c1d-b1f5-60aff91fbeb0
Brennan, Lorraine
efa9251d-9605-48ae-b1b0-27129a4a9270
Puddicombe, Sarah M.
124e2c4e-ab9a-46f3-855c-b54ed0b61cc4
Davies, Donna E.
7de8fdc7-3640-4e3a-aa91-d0e03f990c38
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
December 2001
Chamberlin, Stephen G.
ecb947dd-c59e-4c1d-b1f5-60aff91fbeb0
Brennan, Lorraine
efa9251d-9605-48ae-b1b0-27129a4a9270
Puddicombe, Sarah M.
124e2c4e-ab9a-46f3-855c-b54ed0b61cc4
Davies, Donna E.
7de8fdc7-3640-4e3a-aa91-d0e03f990c38
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Chamberlin, Stephen G., Brennan, Lorraine, Puddicombe, Sarah M., Davies, Donna E. and Turner, David L.
(2001)
Solution structure of the mEGF/TGF ?(44-50) chimeric growth factor.
European Journal of Biochemistry, 268 (23), .
(doi:10.1046/j.0014-2956.2001.02581.x).
Abstract
The solution structure of the growth factor chimera mEGF/TGF ?(44-50) 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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Published date: December 2001
Keywords:
nmr, egf structure, growth factor, indyana, simulated annealing, relaxation matrix approach, factor receptor, factor-? protein structures, tgf-?, biological macromolecules, signal-transduction, chemical-shift, binding
Identifiers
Local EPrints ID: 19447
URI: http://eprints.soton.ac.uk/id/eprint/19447
ISSN: 0014-2956
PURE UUID: 039e0cb8-44b4-4f6c-ab04-a5d7d0416472
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Date deposited: 15 Feb 2006
Last modified: 16 Mar 2024 02:34
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Contributors
Author:
Stephen G. Chamberlin
Author:
Lorraine Brennan
Author:
Sarah M. Puddicombe
Author:
David L. Turner
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