1qau

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(New page: 200px<br /><applet load="1qau" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qau, resolution 1.25&Aring;" /> '''UNEXPECTED MODES OF ...)
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[[Image:1qau.jpg|left|200px]]<br /><applet load="1qau" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qau, resolution 1.25&Aring;" />
caption="1qau, resolution 1.25&Aring;" />
'''UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX'''<br />
'''UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX'''<br />
==Overview==
==Overview==
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The PDZ protein interaction domain of neuronal nitric oxide synthase, (nNOS) can heterodimerize with the PDZ domains of postsynaptic density, protein 95 and syntrophin through interactions that are not mediated by, recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ, complex structure revealed that the domains interact in an unusual linear, head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction, surfaces-one face has the canonical peptide binding groove, whereas the, other has a beta-hairpin "finger." This nNOS beta finger docks in the, syntrophin peptide binding groove, mimicking a peptide ligand, except that, a sharp beta turn replaces the normally required carboxyl terminus. This, structure explains how PDZ domains can participate in diverse interaction, modes to assemble protein networks.
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The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual linear head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide ligand, except that a sharp beta turn replaces the normally required carboxyl terminus. This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks.
==About this Structure==
==About this Structure==
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1QAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QAU OCA].
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1QAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAU OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bredt, D.S.]]
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[[Category: Bredt, D S.]]
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[[Category: Christopherson, K.S.]]
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[[Category: Christopherson, K S.]]
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[[Category: Hillier, B.J.]]
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[[Category: Hillier, B J.]]
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[[Category: Lim, W.A.]]
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[[Category: Lim, W A.]]
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[[Category: Prehoda, K.E.]]
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[[Category: Prehoda, K E.]]
[[Category: beta-finger]]
[[Category: beta-finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:32:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:41 2008''

Revision as of 12:37, 21 February 2008


1qau, resolution 1.25Å

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UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX

Overview

The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual linear head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide ligand, except that a sharp beta turn replaces the normally required carboxyl terminus. This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks.

About this Structure

1QAU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex., Hillier BJ, Christopherson KS, Prehoda KE, Bredt DS, Lim WA, Science. 1999 Apr 30;284(5415):812-5. PMID:10221915

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