1iu2: Difference between revisions

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New page: left|200px<br /><applet load="1iu2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iu2" /> '''The first PDZ domain of PSD-95'''<br /> ==O...
 
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[[Image:1iu2.jpg|left|200px]]<br /><applet load="1iu2" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1iu2.jpg|left|200px]]<br /><applet load="1iu2" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1iu2" />
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'''The first PDZ domain of PSD-95'''<br />
'''The first PDZ domain of PSD-95'''<br />


==Overview==
==Overview==
PDZ domain proteins play critical roles in binding, clustering and, subcellular targeting of membrane receptors and ion channels. PDZ domains, in multi-PDZ proteins often are arranged in groups with highly conserved, spacing and intervening sequences; however, the functional significance of, such tandem arrangements of PDZs is unclear. We have solved the, three-dimensional structure of the first two PDZ domains of postsynaptic, density protein-95 (PSD-95 PDZ1 and PDZ2), which are closely linked to, each other in the PSD-95 family of scaffold proteins. The two PDZs have, limited freedom of rotation and their C-terminal peptide-binding grooves, are aligned with each other with an orientation preference for binding to, pairs of C termini extending in the same direction. Increasing the spacing, between PDZ1 and PDZ2 resulted in decreased binding between PDZ12 and its, dimeric targets. The same mutation impaired the functional ability of, PSD-95 to cluster Kv1.4 potassium channels in heterologous cells. The data, presented provide a molecular basis for preferential binding of PSD-95 to, multimeric membrane proteins with appropriate C-terminal sequences.
PDZ domain proteins play critical roles in binding, clustering and subcellular targeting of membrane receptors and ion channels. PDZ domains in multi-PDZ proteins often are arranged in groups with highly conserved spacing and intervening sequences; however, the functional significance of such tandem arrangements of PDZs is unclear. We have solved the three-dimensional structure of the first two PDZ domains of postsynaptic density protein-95 (PSD-95 PDZ1 and PDZ2), which are closely linked to each other in the PSD-95 family of scaffold proteins. The two PDZs have limited freedom of rotation and their C-terminal peptide-binding grooves are aligned with each other with an orientation preference for binding to pairs of C termini extending in the same direction. Increasing the spacing between PDZ1 and PDZ2 resulted in decreased binding between PDZ12 and its dimeric targets. The same mutation impaired the functional ability of PSD-95 to cluster Kv1.4 potassium channels in heterologous cells. The data presented provide a molecular basis for preferential binding of PSD-95 to multimeric membrane proteins with appropriate C-terminal sequences.


==About this Structure==
==About this Structure==
1IU2 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=1IU2 OCA].  
1IU2 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=1IU2 OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Long, J.F.]]
[[Category: Long, J F.]]
[[Category: Niethammer, M.]]
[[Category: Niethammer, M.]]
[[Category: Sala, C.]]
[[Category: Sala, C.]]
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[[Category: psd-95]]
[[Category: psd-95]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:39:56 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:37 2008''

Revision as of 14:15, 21 February 2008

File:1iu2.jpg


1iu2

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The first PDZ domain of PSD-95

OverviewOverview

PDZ domain proteins play critical roles in binding, clustering and subcellular targeting of membrane receptors and ion channels. PDZ domains in multi-PDZ proteins often are arranged in groups with highly conserved spacing and intervening sequences; however, the functional significance of such tandem arrangements of PDZs is unclear. We have solved the three-dimensional structure of the first two PDZ domains of postsynaptic density protein-95 (PSD-95 PDZ1 and PDZ2), which are closely linked to each other in the PSD-95 family of scaffold proteins. The two PDZs have limited freedom of rotation and their C-terminal peptide-binding grooves are aligned with each other with an orientation preference for binding to pairs of C termini extending in the same direction. Increasing the spacing between PDZ1 and PDZ2 resulted in decreased binding between PDZ12 and its dimeric targets. The same mutation impaired the functional ability of PSD-95 to cluster Kv1.4 potassium channels in heterologous cells. The data presented provide a molecular basis for preferential binding of PSD-95 to multimeric membrane proteins with appropriate C-terminal sequences.

About this StructureAbout this Structure

1IU2 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95., Long JF, Tochio H, Wang P, Fan JS, Sala C, Niethammer M, Sheng M, Zhang M, J Mol Biol. 2003 Mar 14;327(1):203-14. PMID:12614619

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