1jxo: Difference between revisions

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New page: left|200px<br /><applet load="1jxo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxo, resolution 2.30Å" /> '''Crystal Structure of...
 
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[[Image:1jxo.jpg|left|200px]]<br /><applet load="1jxo" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jxo.jpg|left|200px]]<br /><applet load="1jxo" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jxo, resolution 2.30&Aring;" />
caption="1jxo, resolution 2.30&Aring;" />
'''Crystal Structure of the SH3-HOOK-GK Fragment of PSD-95'''<br />
'''Crystal Structure of the SH3-HOOK-GK Fragment of PSD-95'''<br />


==Overview==
==Overview==
PSD-95/SAP90 is a member of the MAGUK superfamily. In excitatory synapses, PSD-95 clusters receptors and ion channels at specific sites in the, postsynaptic membrane and organizes downstream signaling and cytoskeletal, molecules. We have determined the crystal structures of the apo and, GMP-bound forms to 2.3 and 2.0 A resolutions, respectively, of a fragment, containing the SH3, HOOK, and guanylate kinase (GK) domains of PSD-95. We, observe an intramolecular interaction between the SH3 and GK domains, involving the formation of a beta sheet including residues N- and, C-terminal to the GK domain. Based on amino acid conservation and, mutational data available in the literature, we propose that this, intramolecular interaction is a common feature among MAGUK proteins.
PSD-95/SAP90 is a member of the MAGUK superfamily. In excitatory synapses, PSD-95 clusters receptors and ion channels at specific sites in the postsynaptic membrane and organizes downstream signaling and cytoskeletal molecules. We have determined the crystal structures of the apo and GMP-bound forms to 2.3 and 2.0 A resolutions, respectively, of a fragment containing the SH3, HOOK, and guanylate kinase (GK) domains of PSD-95. We observe an intramolecular interaction between the SH3 and GK domains involving the formation of a beta sheet including residues N- and C-terminal to the GK domain. Based on amino acid conservation and mutational data available in the literature, we propose that this intramolecular interaction is a common feature among MAGUK proteins.


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


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brunger, A.T.]]
[[Category: Brunger, A T.]]
[[Category: Panepucci, E.H.]]
[[Category: Panepucci, E H.]]
[[Category: Tavares, G.A.]]
[[Category: Tavares, G A.]]
[[Category: guanylate kinase domain]]
[[Category: guanylate kinase domain]]
[[Category: maguk]]
[[Category: maguk]]
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[[Category: sh3 domain]]
[[Category: sh3 domain]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:40:18 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:51 2008''