PMID- 9678607
OWN - NLM
STAT- MEDLINE
DCOM- 19980825
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 430
IP  - 1-2
DP  - 1998 Jun 23
TI  - Insights into the structure of hepatocyte growth factor/scatter factor (HGF/SF) 
      and implications for receptor activation.
PG  - 126-9
AB  - The modular structure of HGF/SF offers a reductionist or 'divide and rule' 
      approach to the analysis of structure and function. Domain deletion experiments 
      have established that the N domain, kringle 1 and kringle 2 are essential for 
      HGF/SF activity and that truncated variants containing the N domain and kringle 1 
      (NK1) or kringles 1 and 2 (NK2) can exhibit partial agonistic or antagonistic 
      activity depending on target cells. Comparative modelling has been used to 
      predict the 3D structures of the six domains of HGF/SF. More recently, NMR 
      methods have shown that the N domain has a novel fold, the charge distribution of 
      which suggests a heparin binding site. 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.
FAU - Chirgadze, D Y
AU  - Chirgadze DY
AD  - Department of Biochemistry, University of Cambridge, UK.
FAU - Hepple, J
AU  - Hepple J
FAU - Byrd, R A
AU  - Byrd RA
FAU - Sowdhamini, R
AU  - Sowdhamini R
FAU - Blundell, T L
AU  - Blundell TL
FAU - Gherardi, E
AU  - Gherardi E
LA  - eng
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 67256-21-7 (Hepatocyte Growth Factor)
RN  - 9005-49-6 (Heparin)
RN  - EC 2.7.10.1 (Proto-Oncogene Proteins c-met)
SB  - IM
MH  - Binding Sites
MH  - Enzyme Activation
MH  - Heparin/*metabolism
MH  - Hepatocyte Growth Factor/*chemistry/genetics/*metabolism
MH  - Models, Molecular
MH  - Mutagenesis, Site-Directed
MH  - *Protein Conformation
MH  - Proto-Oncogene Proteins c-met/*metabolism
RF  - 26
EDAT- 1998/07/25 00:00
MHDA- 1998/07/25 00:01
CRDT- 1998/07/25 00:00
PHST- 1998/07/25 00:00 [pubmed]
PHST- 1998/07/25 00:01 [medline]
PHST- 1998/07/25 00:00 [entrez]
AID - S0014-5793(98)00558-4 [pii]
AID - 10.1016/s0014-5793(98)00558-4 [doi]
PST - ppublish
SO  - FEBS Lett. 1998 Jun 23;430(1-2):126-9. doi: 10.1016/s0014-5793(98)00558-4.