2i1n: Difference between revisions
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== | ==Crystal structure of the 1st PDZ domain of Human DLG3== | ||
<StructureSection load='2i1n' size='340' side='right'caption='[[2i1n]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2i1n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I1N FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2i1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1n OCA], [https://pdbe.org/2i1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i1n RCSB], [https://www.ebi.ac.uk/pdbsum/2i1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i1n ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/DLG3_HUMAN DLG3_HUMAN] Defects in DLG3 are the cause of mental retardation X-linked type 90 (MRX90) [MIM:[https://omim.org/entry/300850 300850]. Mental retardation is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.<ref>PMID:15185169</ref> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DLG3_HUMAN DLG3_HUMAN] Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling. | |||
== 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/i1/2i1n_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=2i1n ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
PDZ domains are protein-protein interaction modules that generally bind to the C termini of their target proteins. The C-terminal four amino acids of a prospective binding partner of a PDZ domain are typically the determinants of binding specificity. In an effort to determine the structures of a number of PDZ domains we have included appropriate four residue extensions on the C termini of PDZ domain truncation mutants, designed for self-binding. Multiple truncations of each PDZ domain were generated. The four residue extensions, which represent known specificity sequences of the target PDZ domains and cover both class I and II motifs, form intermolecular contacts in the expected manner for the interactions of PDZ domains with protein C termini for both classes. We present the structures of eight unique PDZ domains crystallized using this approach and focus on four which provide information on selectivity (PICK1 and the third PDZ domain of DLG2), binding site flexibility (the third PDZ domain of MPDZ), and peptide-domain interactions (MPDZ 12th PDZ domain). Analysis of our results shows a clear improvement in the chances of obtaining PDZ domain crystals by using this approach compared to similar truncations of the PDZ domains without the C-terminal four residue extensions. | |||
Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions.,Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA Protein Sci. 2007 Apr;16(4):683-94. PMID:17384233<ref>PMID:17384233</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2i1n" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith C]] | ||
[[Category: Berridge | [[Category: Berridge G]] | ||
[[Category: Bunkoczi | [[Category: Bunkoczi G]] | ||
[[Category: Debreczeni | [[Category: Debreczeni J]] | ||
[[Category: Doyle D]] | |||
[[Category: Doyle | [[Category: Edwards A]] | ||
[[Category: Edwards | [[Category: Elkins J]] | ||
[[Category: Elkins | [[Category: Gileadi O]] | ||
[[Category: Gileadi | [[Category: Gorrec F]] | ||
[[Category: Gorrec | [[Category: Phillips C]] | ||
[[Category: Phillips | [[Category: Pike ACW]] | ||
[[Category: Pike | [[Category: Savitsky P]] | ||
[[Category: Sundstrom M]] | |||
[[Category: Savitsky | [[Category: Turnbull AP]] | ||
[[Category: Sundstrom | [[Category: Ugochukwu E]] | ||
[[Category: Turnbull | [[Category: Umeano C]] | ||
[[Category: Ugochukwu | [[Category: Weigelt J]] | ||
[[Category: Umeano | [[Category: Von Delft F]] | ||
[[Category: Weigelt | |||
[[Category: | |||
Latest revision as of 13:04, 30 August 2023
Crystal structure of the 1st PDZ domain of Human DLG3Crystal structure of the 1st PDZ domain of Human DLG3
Structural highlights
DiseaseDLG3_HUMAN Defects in DLG3 are the cause of mental retardation X-linked type 90 (MRX90) [MIM:300850. Mental retardation is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.[1] FunctionDLG3_HUMAN Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPDZ domains are protein-protein interaction modules that generally bind to the C termini of their target proteins. The C-terminal four amino acids of a prospective binding partner of a PDZ domain are typically the determinants of binding specificity. In an effort to determine the structures of a number of PDZ domains we have included appropriate four residue extensions on the C termini of PDZ domain truncation mutants, designed for self-binding. Multiple truncations of each PDZ domain were generated. The four residue extensions, which represent known specificity sequences of the target PDZ domains and cover both class I and II motifs, form intermolecular contacts in the expected manner for the interactions of PDZ domains with protein C termini for both classes. We present the structures of eight unique PDZ domains crystallized using this approach and focus on four which provide information on selectivity (PICK1 and the third PDZ domain of DLG2), binding site flexibility (the third PDZ domain of MPDZ), and peptide-domain interactions (MPDZ 12th PDZ domain). Analysis of our results shows a clear improvement in the chances of obtaining PDZ domain crystals by using this approach compared to similar truncations of the PDZ domains without the C-terminal four residue extensions. Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions.,Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA Protein Sci. 2007 Apr;16(4):683-94. PMID:17384233[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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