1n99: Difference between revisions

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[[Image:1n99.~~gif~~|left|200px]]

[[Image:1n99.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN~~'''~~

===CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12679023}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12679023 is the PubMed ID number.

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==About this Structure==

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[[Category: Otlewski, J.]]

[[Category: Pdz domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:15:16 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:34:46 2008''

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-[[Image:1n99.gif|left|200px]]
+{{Seed}}
+[[Image:1n99.png|left|200px]]
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 {{STRUCTURE_1n99|  PDB=1n99  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12679023}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12679023 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12679023}}
 ==About this Structure==
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 [[Category: Otlewski, J.]]
 [[Category: Pdz domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:15:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:34:46 2008''