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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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References listed in PDB file
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Key reference
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Title
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Insights into function of psi domains from structure of the met receptor psi domain.
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Authors
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G.Kozlov,
A.Perreault,
J.D.Schrag,
M.Park,
M.Cygler,
K.Gehring,
I.Ekiel.
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Ref.
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Biochem Biophys Res Commun, 2004,
321,
234-240.
[DOI no: ]
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PubMed id
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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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