1jxo

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(New page: 200px<br /><applet load="1jxo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxo, resolution 2.30&Aring;" /> '''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"
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[[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==
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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.
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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==
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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].
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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]]
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[[Category: Brunger, A.T.]]
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[[Category: Brunger, A T.]]
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[[Category: Panepucci, E.H.]]
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[[Category: Panepucci, E H.]]
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[[Category: Tavares, G.A.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:40:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:51 2008''

Revision as of 11:27, 21 February 2008


1jxo, resolution 2.30Å

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Crystal Structure of the SH3-HOOK-GK Fragment of PSD-95

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.

About this Structure

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

Reference

Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95., Tavares GA, Panepucci EH, Brunger AT, Mol Cell. 2001 Dec;8(6):1313-25. PMID:11779506

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