7do4: Difference between revisions
New page: '''Unreleased structure''' The entry 7do4 is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of CD97-CD55 complex== | |||
<StructureSection load='7do4' size='340' side='right'caption='[[7do4]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7do4]] is a 2 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=7DO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DO4 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]] 3.2Å</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=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=7do4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7do4 OCA], [https://pdbe.org/7do4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7do4 RCSB], [https://www.ebi.ac.uk/pdbsum/7do4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7do4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AGRE5_HUMAN AGRE5_HUMAN] Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration.[UniProtKB:Q9Z0M6] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The adhesion G protein-coupled receptor CD97 and its ligand complement decay-accelerating factor CD55 are important binding partners in the human immune system. Dysfunction in this binding has been linked to immune disorders such as multiple sclerosis and rheumatoid arthritis, as well as various cancers. Previous literatures have indicated that the CD97 includes 3 to 5 epidermal growth factor (EGF) domains at its N terminus and these EGF domains can bind to the N-terminal short consensus repeat (SCR) domains of CD55. However, the details of this interaction remain elusive, especially why the CD55 binds with the highest affinity to the shortest isoform of CD97 (EGF(1,2,5)). Herein, we designed a chimeric expression construct with the EGF(1,2,5) domains of CD97 and the SCR(1-4) domains of CD55 connected by a flexible linker and determined the complex structure by crystallography. Our data reveal that the two proteins adopt an overall antiparallel binding mode involving the SCR(1-3) domains of CD55 and all three EGF domains of CD97. Mutagenesis data confirmed the importance of EGF(5) in the interaction and explained the binding specificity between CD55 and CD97. The architecture of CD55-CD97 binding mode together with kinetics suggests a force-resisting shearing stretch geometry when forces applied to the C termini of both proteins in the circulating environment. The potential of the CD55-CD97 complex to withstand tensile force may provide a basis for the mechanosensing mechanism for activation of adhesion G protein-coupled receptors. | |||
Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs.,Niu M, Xu S, Yang J, Yao D, Li N, Yan J, Zhong G, Song G J Biol Chem. 2021 Jan-Jun;296:100776. doi: 10.1016/j.jbc.2021.100776. Epub 2021 , May 14. PMID:33992645<ref>PMID:33992645</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7do4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CD55|CD55]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Niu M]] | |||
[[Category: Song G]] | |||
Latest revision as of 19:36, 29 November 2023
Crystal structure of CD97-CD55 complexCrystal structure of CD97-CD55 complex
Structural highlights
FunctionAGRE5_HUMAN Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration.[UniProtKB:Q9Z0M6] Publication Abstract from PubMedThe adhesion G protein-coupled receptor CD97 and its ligand complement decay-accelerating factor CD55 are important binding partners in the human immune system. Dysfunction in this binding has been linked to immune disorders such as multiple sclerosis and rheumatoid arthritis, as well as various cancers. Previous literatures have indicated that the CD97 includes 3 to 5 epidermal growth factor (EGF) domains at its N terminus and these EGF domains can bind to the N-terminal short consensus repeat (SCR) domains of CD55. However, the details of this interaction remain elusive, especially why the CD55 binds with the highest affinity to the shortest isoform of CD97 (EGF(1,2,5)). Herein, we designed a chimeric expression construct with the EGF(1,2,5) domains of CD97 and the SCR(1-4) domains of CD55 connected by a flexible linker and determined the complex structure by crystallography. Our data reveal that the two proteins adopt an overall antiparallel binding mode involving the SCR(1-3) domains of CD55 and all three EGF domains of CD97. Mutagenesis data confirmed the importance of EGF(5) in the interaction and explained the binding specificity between CD55 and CD97. The architecture of CD55-CD97 binding mode together with kinetics suggests a force-resisting shearing stretch geometry when forces applied to the C termini of both proteins in the circulating environment. The potential of the CD55-CD97 complex to withstand tensile force may provide a basis for the mechanosensing mechanism for activation of adhesion G protein-coupled receptors. Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs.,Niu M, Xu S, Yang J, Yao D, Li N, Yan J, Zhong G, Song G J Biol Chem. 2021 Jan-Jun;296:100776. doi: 10.1016/j.jbc.2021.100776. Epub 2021 , May 14. PMID:33992645[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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