3uat

From Proteopedia

(Difference between revisions)

Revision as of 06:05, 13 July 2022

Guanylate Kinase Domains of the MAGUK Family Scaffold Proteins as Specific Phospho-Protein Binding Modules

Structural highlights

3uat is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	Dlg1, Dlgh1 (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DLG1_RAT] Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel (By similarity). May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Membrane-associated guanylate kinases (MAGUKs) are a large family of scaffold proteins that play essential roles in tissue developments, cell-cell communications, cell polarity control, and cellular signal transductions. Despite extensive studies over the past two decades, the functions of the signature guanylate kinase domain (GK) of MAGUKs are poorly understood. Here we show that the GK domain of DLG1/SAP97 binds to asymmetric cell division regulatory protein LGN in a phosphorylation-dependent manner. The structure of the DLG1 SH3-GK tandem in complex with a phospho-LGN peptide reveals that the GMP-binding site of GK has evolved into a specific pSer/pThr-binding pocket. Residues both N- and C-terminal to the pSer are also critical for the specific binding of the phospho-LGN peptide to GK. We further demonstrate that the previously reported GK domain-mediated interactions of DLGs with other targets, such as GKAP/DLGAP1/SAPAP1 and SPAR, are also phosphorylation dependent. Finally, we provide evidence that other MAGUK GKs also function as phospho-peptide-binding modules. The discovery of the phosphorylation-dependent MAGUK GK/target interactions indicates that MAGUK scaffold-mediated signalling complex organizations are dynamically regulated.

Guanylate kinase domains of the MAGUK family scaffold proteins as specific phospho-protein-binding modules.,Zhu J, Shang Y, Xia C, Wang W, Wen W, Zhang M EMBO J. 2011 Nov 25. doi: 10.1038/emboj.2011.428. PMID:22117215^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA. A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels. J Biol Chem. 2004 Apr 30;279(18):19051-63. Epub 2004 Feb 11. PMID:14960569 doi:http://dx.doi.org/10.1074/jbc.M400284200
↑ Mauceri D, Cattabeni F, Di Luca M, Gardoni F. Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines. J Biol Chem. 2004 May 28;279(22):23813-21. Epub 2004 Mar 24. PMID:15044483 doi:http://dx.doi.org/10.1074/jbc.M402796200
↑ Nakagawa T, Futai K, Lashuel HA, Lo I, Okamoto K, Walz T, Hayashi Y, Sheng M. Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions. Neuron. 2004 Oct 28;44(3):453-67. PMID:15504326 doi:http://dx.doi.org/10.1016/j.neuron.2004.10.012
↑ El-Haou S, Balse E, Neyroud N, Dilanian G, Gavillet B, Abriel H, Coulombe A, Jeromin A, Hatem SN. Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes. Circ Res. 2009 Mar 27;104(6):758-69. doi: 10.1161/CIRCRESAHA.108.191007. Epub, 2009 Feb 12. PMID:19213956 doi:10.1161/CIRCRESAHA.108.191007
↑ Zhu J, Shang Y, Xia C, Wang W, Wen W, Zhang M. Guanylate kinase domains of the MAGUK family scaffold proteins as specific phospho-protein-binding modules. EMBO J. 2011 Nov 25. doi: 10.1038/emboj.2011.428. PMID:22117215 doi:10.1038/emboj.2011.428

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3uat"

@@ Line 1: / Line 1: @@
 ==Guanylate Kinase Domains of the MAGUK Family Scaffold Proteins as Specific Phospho-Protein Binding Modules==
-<StructureSection load='3uat' size='340' side='right' caption='[[3uat]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='3uat' size='340' side='right'caption='[[3uat]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3uat]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UAT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3uat]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAT FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dlg1, Dlgh1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dlg1, Dlgh1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3uat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uat OCA], [http://pdbe.org/3uat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uat RCSB], [http://www.ebi.ac.uk/pdbsum/3uat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uat ProSAT]</span></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=3uat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uat OCA], [https://pdbe.org/3uat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uat RCSB], [https://www.ebi.ac.uk/pdbsum/3uat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uat ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DLG1_RAT DLG1_RAT]] Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel (By similarity). May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation.<ref>PMID:14960569</ref> <ref>PMID:15044483</ref> <ref>PMID:15504326</ref> <ref>PMID:19213956</ref>
+[[https://www.uniprot.org/uniprot/DLG1_RAT DLG1_RAT]] Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel (By similarity). May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation.<ref>PMID:14960569</ref> <ref>PMID:15044483</ref> <ref>PMID:15504326</ref> <ref>PMID:19213956</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Buffalo rat]]
+[[Category: Large Structures]]
 [[Category: Shang, Y]]
 [[Category: Wen, W]]

3uat

From Proteopedia

Revision as of 06:05, 13 July 2022

Guanylate Kinase Domains of the MAGUK Family Scaffold Proteins as Specific Phospho-Protein Binding Modules

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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