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Insights into function of PSI domains from structure of the Met receptor PSI domain.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kozlov G,Perreault A,Schrag JD,Park M,Cygler M,Gehring K,Ekiel I

doi

10.1016/j.bbrc.2004.06.132

subject

Has Abstract

pub_date

2004-08-13 00:00:00

pages

234-40

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)01355-5

journal_volume

321

pub_type

杂志文章

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