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1n99
From Proteopedia
(New page: 200px<br /> <applet load="1n99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n99, resolution 1.94Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1n99.gif|left|200px]]<br /> | + | [[Image:1n99.gif|left|200px]]<br /><applet load="1n99" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1n99" size=" | + | |
caption="1n99, resolution 1.94Å" /> | caption="1n99, resolution 1.94Å" /> | ||
'''CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN'''<br /> | '''CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Syntenin, a 33 kDa protein, interacts with several cell membrane receptors | + | Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin. |
==About this Structure== | ==About this Structure== | ||
| - | 1N99 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:// | + | 1N99 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=1N99 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cooper, D | + | [[Category: Cooper, D R.]] |
[[Category: Dauter, Z.]] | [[Category: Dauter, Z.]] | ||
[[Category: Derewenda, U.]] | [[Category: Derewenda, U.]] | ||
| - | [[Category: Derewenda, Z | + | [[Category: Derewenda, Z S.]] |
[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
[[Category: Jelen, F.]] | [[Category: Jelen, F.]] | ||
| - | [[Category: Kang, B | + | [[Category: Kang, B S.]] |
[[Category: Otlewski, J.]] | [[Category: Otlewski, J.]] | ||
[[Category: pdz domain]] | [[Category: pdz domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:41 2008'' |
Revision as of 12:03, 21 February 2008
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CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN
Overview
Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin.
About this Structure
1N99 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
PDZ tandem of human syntenin: crystal structure and functional properties., Kang BS, Cooper DR, Jelen F, Devedjiev Y, Derewenda U, Dauter Z, Otlewski J, Derewenda ZS, Structure. 2003 Apr;11(4):459-68. PMID:12679023
Page seeded by OCA on Thu Feb 21 14:03:41 2008
