PMID- 17662939
OWN - NLM
STAT- MEDLINE
DCOM- 20070913
LR  - 20220408
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 130
IP  - 2
DP  - 2007 Jul 27
TI  - Structure of the human receptor tyrosine kinase met in complex with the Listeria 
      invasion protein InlB.
PG  - 235-46
AB  - The tyrosine kinase Met, the product of the c-met proto-oncogene and the receptor 
      for hepatocyte growth factor/scatter factor (HGF/SF), mediates signals critical 
      for cell survival and migration. The human pathogen Listeria monocytogenes 
      exploits Met signaling for invasion of host cells via its surface protein InlB. 
      We present the crystal structure of the complex between a large fragment of the 
      human Met ectodomain and the Met-binding domain of InlB. The concave face of the 
      InlB leucine-rich repeat region interacts tightly with the first 
      immunoglobulin-like domain of the Met stalk, a domain which does not bind HGF/SF. 
      A second contact between InlB and the Met Sema domain locks the otherwise 
      flexible receptor in a rigid, signaling competent conformation. Full Met 
      activation requires the additional C-terminal domains of InlB which induce 
      heparin-mediated receptor clustering and potent signaling. Thus, although it 
      elicits a similar cellular response, InlB is not a structural mimic of HGF/SF.
FAU - Niemann, Hartmut H
AU  - Niemann HH
AD  - Division of Structural Biology, Helmholtz Centre for Infection Research, 
      Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
FAU - Jager, Volker
AU  - Jager V
FAU - Butler, P Jonathan G
AU  - Butler PJ
FAU - van den Heuvel, Joop
AU  - van den Heuvel J
FAU - Schmidt, Sabine
AU  - Schmidt S
FAU - Ferraris, Davide
AU  - Ferraris D
FAU - Gherardi, Ermanno
AU  - Gherardi E
FAU - Heinz, Dirk W
AU  - Heinz DW
LA  - eng
SI  - PDB/2UZX
SI  - PDB/2UZY
GR  - G9704528/MRC_/Medical Research Council/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Bacterial Proteins)
RN  - 0 (Leucine-Rich Repeat Proteins)
RN  - 0 (MAS1 protein, human)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteins)
RN  - 0 (Proto-Oncogene Mas)
RN  - 0 (inlB protein, Listeria monocytogenes)
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
CIN - Cell. 2007 Jul 27;130(2):218-9. PMID: 17662936
MH  - Bacterial Proteins/*chemistry
MH  - Binding Sites
MH  - Heparin/pharmacology
MH  - Hepatocyte Growth Factor/metabolism
MH  - Humans
MH  - Leucine-Rich Repeat Proteins
MH  - Listeria monocytogenes/*chemistry
MH  - Membrane Proteins/*chemistry
MH  - Models, Biological
MH  - Models, Molecular
MH  - Protein Binding/drug effects
MH  - Protein Interaction Mapping
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Proteins/metabolism
MH  - Proto-Oncogene Mas
MH  - Proto-Oncogene Proteins c-met/*chemistry
EDAT- 2007/07/31 09:00
MHDA- 2007/09/14 09:00
CRDT- 2007/07/31 09:00
PHST- 2007/03/20 00:00 [received]
PHST- 2007/04/20 00:00 [revised]
PHST- 2007/05/11 00:00 [accepted]
PHST- 2007/07/31 09:00 [pubmed]
PHST- 2007/09/14 09:00 [medline]
PHST- 2007/07/31 09:00 [entrez]
AID - S0092-8674(07)00676-9 [pii]
AID - 10.1016/j.cell.2007.05.037 [doi]
PST - ppublish
SO  - Cell. 2007 Jul 27;130(2):235-46. doi: 10.1016/j.cell.2007.05.037.