1ssl
From Proteopedia
(New page: 200px<br /> <applet load="1ssl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ssl" /> '''Solution structure of the PSI domain from t...) |
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'''Solution structure of the PSI domain from the Met receptor'''<br /> | '''Solution structure of the PSI domain from the Met receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PSI domains are cysteine-rich modules found in extracellular fragments of | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1SSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kozlov, G.]] | [[Category: Kozlov, G.]] | ||
[[Category: Perreault, A.]] | [[Category: Perreault, A.]] | ||
| - | [[Category: Schrag, J | + | [[Category: Schrag, J D.]] |
[[Category: cysteine knot]] | [[Category: cysteine knot]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:45 2008'' |
Revision as of 13:04, 21 February 2008
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Solution structure of the PSI domain from the Met receptor
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Autism, suseptibility to, 9 OMIM:[164860], Hepatocellular carcinoma, childhood type OMIM:[164860], Renal cell carcinoma, papillary, familial and sporadic OMIM:[164860]
About this Structure
1SSL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Insights into function of PSI domains from structure of the Met receptor PSI domain., Kozlov G, Perreault A, Schrag JD, Park M, Cygler M, Gehring K, Ekiel I, Biochem Biophys Res Commun. 2004 Aug 13;321(1):234-40. PMID:15358240
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