1n99

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(New page: 200px<br /> <applet load="1n99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n99, resolution 1.94&Aring;" /> '''CRYSTAL STRUCTURE O...)
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caption="1n99, resolution 1.94&Aring;" />
'''CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN'''<br />
'''CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N99 OCA].
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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]]
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[[Category: Cooper, D.R.]]
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[[Category: Cooper, D R.]]
[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
[[Category: Derewenda, U.]]
[[Category: Derewenda, U.]]
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[[Category: Derewenda, Z.S.]]
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[[Category: Derewenda, Z S.]]
[[Category: Devedjiev, Y.]]
[[Category: Devedjiev, Y.]]
[[Category: Jelen, F.]]
[[Category: Jelen, F.]]
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[[Category: Kang, B.S.]]
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[[Category: Kang, B S.]]
[[Category: Otlewski, J.]]
[[Category: Otlewski, J.]]
[[Category: pdz domain]]
[[Category: pdz domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:19:19 2007''
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''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


1n99, resolution 1.94Å

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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

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