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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kpk]] 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=2KPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KPK FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kpk]] 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=2KPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KPK FirstGlance]. <br>
</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=2kpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kpk OCA], [https://pdbe.org/2kpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kpk RCSB], [https://www.ebi.ac.uk/pdbsum/2kpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kpk ProSAT]</span></td></tr>
</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=2kpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kpk OCA], [https://pdbe.org/2kpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kpk RCSB], [https://www.ebi.ac.uk/pdbsum/2kpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kpk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/MAGI1_HUMAN MAGI1_HUMAN] May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity).
[https://www.uniprot.org/uniprot/MAGI1_HUMAN MAGI1_HUMAN] May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PDZ domains are protein interaction domains that are found in cytoplasmic proteins involved in signaling pathways and subcellular transport. Their roles in the control of cell growth, cell polarity, and cell adhesion in response to cell contact render this family of proteins targets during the development of cancer. Targeting of these network hubs by the oncoprotein E6 of "high-risk" human papillomaviruses (HPVs) serves to effect the efficient disruption of cellular processes. Using NMR, we have solved the three-dimensional solution structure of an extended construct of the second PDZ domain of MAGI-1 (MAGI-1 PDZ1) alone and bound to a peptide derived from the C-terminus of HPV16 E6, and we have characterized the changes in backbone dynamics and hydrogen bonding that occur upon binding. The binding event induces quenching of high-frequency motions in the C-terminal tail of the PDZ domain, which contacts the peptide upstream of the canonical X-[T/S]-X-[L/V] binding motif. Mutations designed in the C-terminal flanking region of the PDZ domain resulted in a significant decrease in binding affinity for E6 peptides. This detailed analysis supports the notion of a global response of the PDZ domain to the binding event, with effects propagated to distal sites, and reveals unexpected roles for the sequences flanking the canonical PDZ domain boundaries.
The Structural and Dynamic Response of MAGI-1 PDZ1 with Noncanonical Domain Boundaries to the Binding of Human Papillomavirus E6.,Charbonnier S, Nomine Y, Ramirez J, Luck K, Chapelle A, Stote RH, Trave G, Kieffer B, Atkinson RA J Mol Biol. 2011 Jan 13. PMID:21238461<ref>PMID:21238461</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kpk" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]]
*[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>
Retrieved from "https://proteopedia.org/2kpk"