1kef

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1kef" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kef" /> '''PDZ1 of SAP90'''<br /> ==Overview== The st...)
Current revision (08:41, 22 May 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1kef.gif|left|200px]]<br />
 
-
<applet load="1kef" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1kef" />
 
-
'''PDZ1 of SAP90'''<br />
 
-
==Overview==
+
==PDZ1 of SAP90==
-
The structural features of the PDZ1 domain of the synapse-associated, protein SAP90 have been characterized by NMR. A comparison with the, structures of the PDZ2 and PDZ3 domains of SAP90 illustrates significant, differences, which may account for the unique binding properties of these, homologous domains. Within the postsynaptic density, SAP90 functions as a, molecular scaffold with a number of the protein-protein interactions, mediated through the PDZ1 domain. Here, using fluorescence anisotropy and, NMR chemical shift analysis, we have characterized the association of PDZ1, to the C-terminal peptides of the GluR6 subunit of the kainate receptor, voltage-gated K(+) channel Kv1.4, and microtubule-associate protein CRIPT, all of which are known to associate with SAP90. The latter two, which, possess the consensus sequence for binding to PDZ domains (T/S-X-V-oh), have low micromolar binding affinities (1.5-15 microm). The C terminus of, GluR6, RLPGKETMA-oh, lacking the consensus sequence, binds to PDZ1 of, SAP90 with an affinity of 160 microm. The NMR data illustrate that, although all three peptides occupy the binding groove capped by the GLGF, loop of PDZ1, specific differences are present, consistent with the, variation in binding affinities.
+
<StructureSection load='1kef' size='340' side='right'caption='[[1kef]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1kef]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KEF FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kef OCA], [https://pdbe.org/1kef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kef RCSB], [https://www.ebi.ac.uk/pdbsum/1kef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kef ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DLG4_HUMAN DLG4_HUMAN] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B (By similarity).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ke/1kef_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kef ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The structural features of the PDZ1 domain of the synapse-associated protein SAP90 have been characterized by NMR. A comparison with the structures of the PDZ2 and PDZ3 domains of SAP90 illustrates significant differences, which may account for the unique binding properties of these homologous domains. Within the postsynaptic density, SAP90 functions as a molecular scaffold with a number of the protein-protein interactions mediated through the PDZ1 domain. Here, using fluorescence anisotropy and NMR chemical shift analysis, we have characterized the association of PDZ1 to the C-terminal peptides of the GluR6 subunit of the kainate receptor, voltage-gated K(+) channel Kv1.4, and microtubule-associate protein CRIPT, all of which are known to associate with SAP90. The latter two, which possess the consensus sequence for binding to PDZ domains (T/S-X-V-oh), have low micromolar binding affinities (1.5-15 microm). The C terminus of GluR6, RLPGKETMA-oh, lacking the consensus sequence, binds to PDZ1 of SAP90 with an affinity of 160 microm. The NMR data illustrate that although all three peptides occupy the binding groove capped by the GLGF loop of PDZ1, specific differences are present, consistent with the variation in binding affinities.
-
==About this Structure==
+
The PDZ1 domain of SAP90. Characterization of structure and binding.,Piserchio A, Pellegrini M, Mehta S, Blackman SM, Garcia EP, Marshall J, Mierke DF J Biol Chem. 2002 Mar 1;277(9):6967-73. Epub 2001 Dec 14. PMID:11744724<ref>PMID:11744724</ref>
-
1KEF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KEF OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
The PDZ1 domain of SAP90. Characterization of structure and binding., Piserchio A, Pellegrini M, Mehta S, Blackman SM, Garcia EP, Marshall J, Mierke DF, J Biol Chem. 2002 Mar 1;277(9):6967-73. Epub 2001 Dec 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11744724 11744724]
+
</div>
 +
<div class="pdbe-citations 1kef" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Blackman, S.M.]]
+
[[Category: Blackman SM]]
-
[[Category: Garcia, E.P.]]
+
[[Category: Garcia EP]]
-
[[Category: Marshall, J.]]
+
[[Category: Marshall J]]
-
[[Category: Mehta, S.]]
+
[[Category: Mehta S]]
-
[[Category: Mierke, D.F.]]
+
[[Category: Mierke DF]]
-
[[Category: Pellegrini, M.]]
+
[[Category: Pellegrini M]]
-
[[Category: Piserchio, A.]]
+
[[Category: Piserchio A]]
-
[[Category: anti-parallel beta-sandwich]]
+
-
[[Category: beta-sheet]]
+
-
[[Category: glgf loop]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:50:26 2007''
+

Current revision

PDZ1 of SAP90

PDB ID 1kef

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kef"
Personal tools