9p99: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==CryoEM structure of integrin alphaEbeta7 bound to E-cadherin== | |||
<StructureSection load='9p99' size='340' side='right'caption='[[9p99]], [[Resolution|resolution]] 3.37Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9p99]] is a 3 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=9P99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9P99 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.37Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=9p99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9p99 OCA], [https://pdbe.org/9p99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9p99 RCSB], [https://www.ebi.ac.uk/pdbsum/9p99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9p99 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ITAE_HUMAN ITAE_HUMAN] Integrin alpha-E/beta-7 is a receptor for E-cadherin. It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Integrins bind ligands between their alpha (alpha) and beta (beta) subunits and transmit signals through conformational changes. Early in chordate evolution, some alpha subunits acquired an "inserted" (I) domain that expanded integrin's ligand-binding repertoire but obstructed the ancestral ligand pocket, seemingly blocking conventional integrin activation. Here, we compare cryo-electron microscopy structures of apo and ligand-bound states of the I domain-containing alphaEbeta(7) integrin and the I domain-lacking alpha(4)beta(7) integrin to illuminate how the I domain intrinsically mimics an extrinsic ligand to preserve integrin function. We trace the I domain's evolutionary origin to an ancestral collagen-collagen interaction domain, identifying an ancient molecular exaptation that facilitated integrin activation immediately upon I domain insertion. Our analyses reveal the evolutionary and biochemical basis of expanded cellular communication in vertebrates. | |||
Molecular exaptation by the integrin alphaI domain.,Hollis JA, Chan MC, Malik HS, Campbell MG Sci Adv. 2025 Sep 12;11(37):eadx9567. doi: 10.1126/sciadv.adx9567. Epub 2025 Sep , 10. PMID:40929264<ref>PMID:40929264</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9p99" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Campbell MG]] | |||
[[Category: Hollis JA]] | |||
Latest revision as of 05:47, 24 September 2025
CryoEM structure of integrin alphaEbeta7 bound to E-cadherin
| ||||||||||||
