PDBsum entry 1ssl

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protein links
Structural protein PDB id
Jmol PyMol
Protein chain
48 a.a. *
* Residue conservation analysis
PDB id:
Name: Structural protein
Title: Solution structure of the psi domain from the met receptor
Structure: 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
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: G.Kozlov,A.Perreault,J.D.Schrag,M.Cygler,K.Gehring,I.Ekiel
Key ref: 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: 15358240 DOI: 10.1016/j.bbrc.2004.06.132
24-Mar-04     Release date:   12-Oct-04    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P08581  (MET_HUMAN) -  Hepatocyte growth factor receptor
1390 a.a.
48 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
+ [protein]-L-tyrosine
+ [protein]-L-tyrosine phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 


DOI no: 10.1016/j.bbrc.2004.06.132 Biochem Biophys Res Commun 321:234-240 (2004)
PubMed id: 15358240  
Insights into function of PSI domains from structure of the Met receptor PSI domain.
G.Kozlov, A.Perreault, J.D.Schrag, M.Park, M.Cygler, K.Gehring, I.Ekiel.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20230529 D.Dotzauer, S.Wolfenstetter, D.Eibert, S.Schneider, P.Dietrich, and N.Sauer (2010).
Novel PSI domains in plant and animal H+-inositol symporters.
  Traffic, 11, 767-781.  
18495663 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.
  J Biol Chem, 283, 21267-21277.  
17117435 A.C.Wozniak, and J.E.Anderson (2007).
Nitric oxide-dependence of satellite stem cell activation and quiescence on normal skeletal muscle fibers.
  Dev Dyn, 236, 240-250.  
15557320 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.
  J Biol Chem, 280, 4238-4246.  
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.