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PDBsum entry 1ssl
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Structural protein
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PDB id
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1ssl
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Contents |
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* Residue conservation analysis
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PDB id:
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Structural protein
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Title:
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Solution structure of the psi domain from the met receptor
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Structure:
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Hepatocyte growth factor receptor. Chain: a. Fragment: psi domain (residues 519-562). Synonym: met proto-oncogene tyrosine kinase, c-met, hgf receptor, hgf-sf receptor. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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G.Kozlov,A.Perreault,J.D.Schrag,M.Cygler,K.Gehring,I.Ekiel
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Key ref:
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G.Kozlov
et al.
(2004).
Insights into function of PSI domains from structure of the Met receptor PSI domain.
Biochem Biophys Res Commun,
321,
234-240.
PubMed id:
DOI:
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Date:
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24-Mar-04
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Release date:
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12-Oct-04
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PROCHECK
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Headers
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References
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P08581
(MET_HUMAN) -
Hepatocyte growth factor receptor from Homo sapiens
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Seq:
Struc:
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1390 a.a.
48 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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Enzyme class:
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E.C.2.7.10.1
- receptor protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Biochem Biophys Res Commun
321:234-240
(2004)
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PubMed id:
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Insights into function of PSI domains from structure of the Met receptor PSI domain.
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G.Kozlov,
A.Perreault,
J.D.Schrag,
M.Park,
M.Cygler,
K.Gehring,
I.Ekiel.
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ABSTRACT
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PSI domains are cysteine-rich modules found in extracellular fragments of
hundreds of signaling proteins, including plexins, semaphorins, integrins, and
attractins. Here, we report the solution structure of the PSI domain from the
human Met receptor, a receptor tyrosine kinase critical for proliferation,
motility, and differentiation. The structure represents a cysteine knot with
short regions of secondary structure including a three-stranded antiparallel
beta-sheet and two alpha-helices. All eight cysteines are involved in disulfide
bonds with the pattern consistent with that for the PSI domain from Sema4D.
Comparison with the Sema4D structure identifies a structurally conserved core
comprising the N-terminal half of the PSI domain. Interestingly, this part links
adjacent SEMA and immunoglobulin domains in the Sema4D structure, suggesting
that the PSI domain serves as a wedge between propeller and immunoglobulin
domains and is responsible for the correct positioning of the ligand-binding
site of the receptor.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Dotzauer,
S.Wolfenstetter,
D.Eibert,
S.Schneider,
P.Dietrich,
and
N.Sauer
(2010).
Novel PSI domains in plant and animal H+-inositol symporters.
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Traffic,
11,
767-781.
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C.Basilico,
A.Arnesano,
M.Galluzzo,
P.M.Comoglio,
and
P.Michieli
(2008).
A high affinity hepatocyte growth factor-binding site in the immunoglobulin-like region of Met.
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J Biol Chem,
283,
21267-21277.
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A.C.Wozniak,
and
J.E.Anderson
(2007).
Nitric oxide-dependence of satellite stem cell activation and quiescence on normal skeletal muscle fibers.
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Dev Dyn,
236,
240-250.
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A.P.Mould,
M.A.Travis,
S.J.Barton,
J.A.Hamilton,
J.A.Askari,
S.E.Craig,
P.R.Macdonald,
R.A.Kammerer,
P.A.Buckley,
and
M.J.Humphries
(2005).
Evidence that monoclonal antibodies directed against the integrin beta subunit plexin/semaphorin/integrin domain stimulate function by inducing receptor extension.
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J Biol Chem,
280,
4238-4246.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
