7lxe: Difference between revisions
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==ENAH EVH1 domain bound to peptide from ABI1== | ==ENAH EVH1 domain bound to peptide from ABI1== | ||
<StructureSection load='7lxe' size='340' side='right'caption='[[7lxe]]' scene=''> | <StructureSection load='7lxe' size='340' side='right'caption='[[7lxe]], [[Resolution|resolution]] 1.88Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXE FirstGlance]. <br> | <table><tr><td colspan='2'>[[7lxe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXE 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=7lxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxe OCA], [https://pdbe.org/7lxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxe RCSB], [https://www.ebi.ac.uk/pdbsum/7lxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxe ProSAT]</span></td></tr> | </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=7lxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxe OCA], [https://pdbe.org/7lxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxe RCSB], [https://www.ebi.ac.uk/pdbsum/7lxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human proteome is replete with short linear motifs (SLiMs) of four to six residues that are critical for protein-protein interactions, yet the importance of the sequence surrounding such motifs is underexplored. We devised a proteomic screen to examine the influence of SLiM sequence context on protein-protein interactions. Focusing on the EVH1 domain of human ENAH, an actin regulator that is highly expressed in invasive cancers, we screened 36-residue proteome-derived peptides and discovered new interaction partners of ENAH and diverse mechanisms by which context influences binding. A pocket on the ENAH EVH1 domain that has diverged from other Ena/VASP paralogs recognizes extended SLiMs and favors motif-flanking proline residues. Many high-affinity ENAH binders that contain two proline-rich SLiMs use a noncanonical site on the EVH1 domain for binding and display a thermodynamic signature consistent with the two-motif chain engaging a single domain. We also found that photoreceptor cilium actin regulator (PCARE) uses an extended 23-residue region to obtain a higher affinity than any known ENAH EVH1-binding motif. Our screen provides a way to uncover the effects of proteomic context on motif-mediated binding, revealing diverse mechanisms of control over EVH1 interactions and establishing that SLiMs can't be fully understood outside of their native context. | |||
Native proline-rich motifs exploit sequence context to target actin-remodeling Ena/VASP protein ENAH.,Hwang T, Parker SS, Hill SM, Grant RA, Ilunga MW, Sivaraman V, Mouneimne G, Keating AE Elife. 2022 Jan 25;11. pii: 70680. doi: 10.7554/eLife.70680. PMID:35076015<ref>PMID:35076015</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7lxe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Grant | [[Category: Grant, R A]] | ||
[[Category: Hwang | [[Category: Hwang, T H]] | ||
[[Category: Keating | [[Category: Keating, A E]] | ||
[[Category: Complex]] | |||
[[Category: Cytoskeleton]] | |||
[[Category: Protein binding]] | |||
Revision as of 05:07, 10 August 2022
ENAH EVH1 domain bound to peptide from ABI1
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