Jonathan Hepple
University of Cambridge
5 Papers
158 Citations
Jonathan Hepple is an academic researcher from University of Cambridge. The author has contributed to research in topics: Hepatocyte growth factor & Receptor tyrosine kinase. The author has an hindex of 4, co-authored 5 publications.
Chat about Author
Papers
Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding.
TL;DR: The crystal structure of NK1, a receptor-binding fragment and a natural splice variant of hepatocyte growth factor/scatter factor (HGF/SF), reveals a novel mode of growth factor dimerization produced by close packing of the N domain of one subunit and the kringle domain of the other, thus bringing the two linkers in close proximity.
120
Insights into the structure of hepatocyte growth factor/scatter factor (hgf/sf) and implications for receptor activation
Dimitri Y. Chirgadze,Jonathan Hepple,R. Andrew Byrd,Ramanathan Sowdhamini,Tom L. Blundell,Ermanno Gherardi +5 more
TL;DR: Crystals of NK1 indicate the relationship of this domain to the kringle 1, offering further insights into the mechanism of domain interactions and receptor activation.
35
Domain structure of hepatocyte growth factor/scatter factor (HGF/SF).
Ermanno Gherardi,Guido Hartmann,Jonathan Hepple,Dimitri Y. Chirgadze,Narayanaswamy Srinivasan,Tom L. Blundell +5 more
- 01 Jan 1997
TL;DR: The modular structure of hepatocyte growth factor/scatter factor (HGF/SF) has facilitated structure-function analysis as mentioned in this paper, and the 3D structures of the six domains of HGF were modelled on the structure of homologues, offering interesting insights into putative mechanisms of domain interactions, receptor binding and activation.
6
Engineered mutants of HGF/SF with reduced binding to heparan sulphate proteoglycans, decreased clearance and enhanced activity in vivo
Guido Hartmann,Terence Prospero,Volker Brinkmann,Öemil Ozcelik,Greg Winter,Jonathan Hepple,Sarah Batley,Friedhelm Bladt,Martin Sachs,Carmen Birchmeier,Walter Birchmeier,Ermanno Gherardi +11 more
TL;DR: The results establish the following: the binding sites in HGF/SF for Met and for HSPGs can be dissociated by protein engineering; high-affinity binding of H GF/SF to H SPGs is not essential for signalling; one role of HSPG binding in the HGF /SF system appears to be sequestration and degradation of the growth factor.