3on9: Difference between revisions
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The | ==The SECRET domain from Ectromelia virus== | ||
<StructureSection load='3on9' size='340' side='right'caption='[[3on9]], [[Resolution|resolution]] 1.57Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3on9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ectromelia_virus Ectromelia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ON9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ON9 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]] 1.57Å</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=3on9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3on9 OCA], [https://pdbe.org/3on9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3on9 RCSB], [https://www.ebi.ac.uk/pdbsum/3on9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3on9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7TDW8_9POXV Q7TDW8_9POXV] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pathogens have evolved sophisticated mechanisms to evade detection and destruction by the host immune system. Large DNA viruses encode homologues of chemokines and their receptors, as well as chemokine-binding proteins (CKBPs) to modulate the chemokine network in host response. The SECRET domain (smallpox virus-encoded chemokine receptor) represents a new family of viral CKBPs that binds a subset of chemokines from different classes to inhibit their activities, either independently or fused with viral tumor necrosis factor receptors (vTNFRs). Here we present the crystal structures of the SECRET domain of vTNFR CrmD encoded by ectromelia virus and its complex with chemokine CX3CL1. The SECRET domain adopts a beta-sandwich fold and utilizes its beta-sheet I surface to interact with CX3CL1, representing a new chemokine-binding manner of viral CKBPs. Structure-based mutagenesis and biochemical analysis identified important basic residues in the 40s loop of CX3CL1 for the interaction. Mutation of corresponding acidic residues in the SECRET domain also affected the binding for other chemokines, indicating that the SECRET domain binds different chemokines in a similar manner. We further showed that heparin inhibited the binding of CX3CL1 by the SECRET domain and the SECRET domain inhibited RAW264.7 cell migration induced by CX3CL1. These results together shed light on the structural basis for the SECRET domain to inhibit chemokine activities by interfering with both chemokine-GAG and chemokine-receptor interactions. | |||
Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor.,Xue X, Lu Q, Wei H, Wang D, Chen D, He G, Huang L, Wang H, Wang X PLoS Pathog. 2011 Jul;7(7):e1002162. Epub 2011 Jul 28. PMID:21829356<ref>PMID:21829356</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3on9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ectromelia virus]] | |||
[[Category: Large Structures]] | |||
[[Category: Wang DL]] | |||
[[Category: Wang XQ]] | |||
[[Category: Xue XG]] | |||
Latest revision as of 11:05, 9 October 2024
The SECRET domain from Ectromelia virusThe SECRET domain from Ectromelia virus
Structural highlights
FunctionPublication Abstract from PubMedPathogens have evolved sophisticated mechanisms to evade detection and destruction by the host immune system. Large DNA viruses encode homologues of chemokines and their receptors, as well as chemokine-binding proteins (CKBPs) to modulate the chemokine network in host response. The SECRET domain (smallpox virus-encoded chemokine receptor) represents a new family of viral CKBPs that binds a subset of chemokines from different classes to inhibit their activities, either independently or fused with viral tumor necrosis factor receptors (vTNFRs). Here we present the crystal structures of the SECRET domain of vTNFR CrmD encoded by ectromelia virus and its complex with chemokine CX3CL1. The SECRET domain adopts a beta-sandwich fold and utilizes its beta-sheet I surface to interact with CX3CL1, representing a new chemokine-binding manner of viral CKBPs. Structure-based mutagenesis and biochemical analysis identified important basic residues in the 40s loop of CX3CL1 for the interaction. Mutation of corresponding acidic residues in the SECRET domain also affected the binding for other chemokines, indicating that the SECRET domain binds different chemokines in a similar manner. We further showed that heparin inhibited the binding of CX3CL1 by the SECRET domain and the SECRET domain inhibited RAW264.7 cell migration induced by CX3CL1. These results together shed light on the structural basis for the SECRET domain to inhibit chemokine activities by interfering with both chemokine-GAG and chemokine-receptor interactions. Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor.,Xue X, Lu Q, Wei H, Wang D, Chen D, He G, Huang L, Wang H, Wang X PLoS Pathog. 2011 Jul;7(7):e1002162. Epub 2011 Jul 28. PMID:21829356[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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