1qau
From Proteopedia
(New page: 200px<br /><applet load="1qau" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qau, resolution 1.25Å" /> '''UNEXPECTED MODES OF ...) |
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- | [[Image:1qau.jpg|left|200px]]<br /><applet load="1qau" size=" | + | [[Image:1qau.jpg|left|200px]]<br /><applet load="1qau" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qau, resolution 1.25Å" /> | caption="1qau, resolution 1.25Å" /> | ||
'''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== | ||
- | The PDZ protein interaction domain of neuronal nitric oxide synthase | + | 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== | ||
- | 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:// | + | 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]] | ||
- | [[Category: Bredt, D | + | [[Category: Bredt, D S.]] |
- | [[Category: Christopherson, K | + | [[Category: Christopherson, K S.]] |
- | [[Category: Hillier, B | + | [[Category: Hillier, B J.]] |
- | [[Category: Lim, W | + | [[Category: Lim, W A.]] |
- | [[Category: Prehoda, K | + | [[Category: Prehoda, K E.]] |
[[Category: beta-finger]] | [[Category: beta-finger]] | ||
- | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 14:37:41 2008