View source for 6twq


==MAGI1_2 complexed with a 16E6 peptide==
<StructureSection load='6twq' size='340' side='right'caption='[[6twq]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6twq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_papillomavirus_type_16 Human papillomavirus type 16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TWQ 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]] 2.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6twq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6twq OCA], [https://pdbe.org/6twq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6twq RCSB], [https://www.ebi.ac.uk/pdbsum/6twq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6twq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H7C535_HUMAN H7C535_HUMAN] [https://www.uniprot.org/uniprot/ANXA2_HUMAN ANXA2_HUMAN] Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response.
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== Publication Abstract from PubMed ==
Protein-protein interaction motifs are often alterable by post-translational modifications. For example, 19% of predicted human PDZ domain-binding motifs (PBMs) have been experimentally proven to be phosphorylated, and up to 82% are theoretically phosphorylatable. Phosphorylation of PBMs may drastically rewire their interactomes, by altering their affinities for PDZ domains and 14-3-3 proteins. The effect of phosphorylation is often analyzed by performing "phosphomimetic" mutations. Here, we focused on the PBMs of HPV16-E6 viral oncoprotein and human RSK1 kinase. We measured the binding affinities of native, phosphorylated, and phosphomimetic variants of both PBMs toward the 266 human PDZ domains. We co-crystallized all the motif variants with a selected PDZ domain to characterize the structural consequence of the different modifications. Finally, we elucidated the structural basis of PBM capture by 14-3-3 proteins. This study provides novel atomic and interactomic insights into phosphorylatable dual specificity motifs and the differential effects of phosphorylation and phosphomimetic approaches.

Dual Specificity PDZ- and 14-3-3-Binding Motifs: A Structural and Interactomics Study.,Gogl G, Jane P, Caillet-Saguy C, Kostmann C, Bich G, Cousido-Siah A, Nyitray L, Vincentelli R, Wolff N, Nomine Y, Sluchanko NN, Trave G Structure. 2020 Apr 6. pii: S0969-2126(20)30092-7. doi:, 10.1016/j.str.2020.03.010. PMID:32294469<ref>PMID:32294469</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6twq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human papillomavirus type 16]]
[[Category: Large Structures]]
[[Category: Cousido-Siah A]]
[[Category: Gogl G]]
[[Category: Trave G]]