This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7lxf
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
==ENAH EVH1 domain bound to peptide from protein PCARE== | ==ENAH EVH1 domain bound to peptide from protein PCARE== | ||
| - | <StructureSection load='7lxf' size='340' side='right'caption='[[7lxf]]' scene=''> | + | <StructureSection load='7lxf' size='340' side='right'caption='[[7lxf]], [[Resolution|resolution]] 1.65Å' 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=7LXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7lxf]] is a 1 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=7LXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXF 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=7lxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxf OCA], [https://pdbe.org/7lxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxf RCSB], [https://www.ebi.ac.uk/pdbsum/7lxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxf ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</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=7lxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxf OCA], [https://pdbe.org/7lxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxf RCSB], [https://www.ebi.ac.uk/pdbsum/7lxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/PCARE_HUMAN PCARE_HUMAN] Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PCARE_HUMAN PCARE_HUMAN] Plays an essential role for normal photoreceptor cell maintenance and vision.<ref>PMID:20398886</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metazoan proteomes contain many paralogous proteins that have evolved distinct functions. The Ena/VASP family of actin regulators consists of three members that share an EVH1 interaction domain with a 100 % conserved binding site. A proteome-wide screen revealed photoreceptor cilium actin regulator (PCARE) as a high-affinity ligand for ENAH EVH1. Here, we report the surprising observation that PCARE is ~100-fold specific for ENAH over paralogs VASP and EVL and can selectively bind ENAH and inhibit ENAH-dependent adhesion in cells. Specificity arises from a mechanism whereby PCARE stabilizes a conformation of the ENAH EVH1 domain that is inaccessible to family members VASP and EVL. Structure-based modeling rapidly identified seven residues distributed throughout EVL that are sufficient to differentiate binding by ENAH vs. EVL. By exploiting the ENAH-specific conformation, we rationally designed the tightest and most selective ENAH binder to date. Our work uncovers a conformational mechanism of interaction specificity that distinguishes highly similar paralogs and establishes tools for dissecting specific Ena/VASP functions in processes including cancer cell invasion. | ||
| + | |||
| + | A distributed residue network permits conformational binding specificity in a conserved family of actin remodelers.,Hwang T, Parker SS, Hill SM, Ilunga MW, Grant RA, Mouneimne G, Keating AE Elife. 2021 Dec 2;10. pii: 70601. doi: 10.7554/eLife.70601. PMID:34854809<ref>PMID:34854809</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7lxf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Grant RA]] | [[Category: Grant RA]] | ||
[[Category: Hwang T]] | [[Category: Hwang T]] | ||
[[Category: Keating AE]] | [[Category: Keating AE]] | ||
Current revision
ENAH EVH1 domain bound to peptide from protein PCARE
| |||||||||||
