1p1d: Difference between revisions

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New page: left|200px<br /><applet load="1p1d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p1d" /> '''Structural Insights into the Inter-domain Ch...
 
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[[Image:1p1d.gif|left|200px]]<br /><applet load="1p1d" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1p1d.gif|left|200px]]<br /><applet load="1p1d" size="350" color="white" frame="true" align="right" spinBox="true"  
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'''Structural Insights into the Inter-domain Chaperoning of Tandem PDZ Domains in Glutamate Receptor Interacting Proteins'''<br />
'''Structural Insights into the Inter-domain Chaperoning of Tandem PDZ Domains in Glutamate Receptor Interacting Proteins'''<br />


==Overview==
==Overview==
The interaction of the glutamate receptor subunits 2 and 3 (GluR2/3) with, multi-PDZ domain glutamate receptor-interacting protein (GRIP) is, important for the synaptic trafficking and clustering of the receptors., Binding of GluR2/3 to GRIP requires both the fourth and fifth PDZ domains, (PDZ4 and PDZ5) to be covalently linked, although only one PDZ domain is, directly involved in binding to the receptor tail. To elucidate the, molecular basis of this mode of PDZ domain-mediated target recognition, we, solved the solution structures of the PDZ45 tandem and the isolated PDZ4, of GRIP. The two PDZ domains form a compact structure with a fixed, interdomain orientation. The interdomain packing and the stable folding of, both PDZ domains require a short stretch of amino acids N-terminal to PDZ4, and a conserved linker connecting PDZ4 and PDZ5. PDZ4 contains a deformed, aB-bB groove that is unlikely to bind to carboxyl peptides. Instead, the, domain stabilizes the structure of PDZ5.
The interaction of the glutamate receptor subunits 2 and 3 (GluR2/3) with multi-PDZ domain glutamate receptor-interacting protein (GRIP) is important for the synaptic trafficking and clustering of the receptors. Binding of GluR2/3 to GRIP requires both the fourth and fifth PDZ domains (PDZ4 and PDZ5) to be covalently linked, although only one PDZ domain is directly involved in binding to the receptor tail. To elucidate the molecular basis of this mode of PDZ domain-mediated target recognition, we solved the solution structures of the PDZ45 tandem and the isolated PDZ4 of GRIP. The two PDZ domains form a compact structure with a fixed interdomain orientation. The interdomain packing and the stable folding of both PDZ domains require a short stretch of amino acids N-terminal to PDZ4 and a conserved linker connecting PDZ4 and PDZ5. PDZ4 contains a deformed aB-bB groove that is unlikely to bind to carboxyl peptides. Instead, the domain stabilizes the structure of PDZ5.


==About this Structure==
==About this Structure==
1P1D 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=1P1D OCA].  
1P1D 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=1P1D OCA].  


==Reference==
==Reference==
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[[Category: tandem repeats]]
[[Category: tandem repeats]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:03 2008''