1z7z

From Proteopedia

(Difference between revisions)

Revision as of 16:58, 20 October 2021

Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi

1z7z, resolution 8.00Å

Structural highlights

1z7z is a 6 chain structure with sequence from Homo sapiens and Human coxsackievirus a21. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1iam, 1z7s
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ICAM1_HUMAN] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

CVA21 and polioviruses both belong to the Enterovirus genus in the family of Picornaviridae, whereas rhinoviruses form a distinct picornavirus genus. Nevertheless, CVA21 and the major group of human rhinoviruses recognize intercellular adhesion molecule-1 (ICAM-1) as their cellular receptor, whereas polioviruses use poliovirus receptor. The crystal structure of CVA21 has been determined to 3.2 A resolution. Its structure has greater similarity to poliovirus structures than to other known picornavirus structures. Cryo-electron microscopy (cryo-EM) was used to determine an 8.0 A resolution structure of CVA21 complexed with an ICAM-1 variant, ICAM-1(Kilifi). The cryo-EM map was fitted with the crystal structures of ICAM-1 and CVA21. Significant differences in the structure of CVA21 with respect to the poliovirus structures account for the inability of ICAM-1 to bind polioviruses. The interface between CVA21 and ICAM-1 has shape and electrostatic complementarity with many residues being conserved among those CVAs that bind ICAM-1.

The crystal structure of coxsackievirus A21 and its interaction with ICAM-1.,Xiao C, Bator-Kelly CM, Rieder E, Chipman PR, Craig A, Kuhn RJ, Wimmer E, Rossmann MG Structure. 2005 Jul;13(7):1019-33. PMID:16004874^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Greve JM, Davis G, Meyer AM, Forte CP, Yost SC, Marlor CW, Kamarck ME, McClelland A. The major human rhinovirus receptor is ICAM-1. Cell. 1989 Mar 10;56(5):839-47. PMID:2538243
↑ Marlin SD, Staunton DE, Springer TA, Stratowa C, Sommergruber W, Merluzzi VJ. A soluble form of intercellular adhesion molecule-1 inhibits rhinovirus infection. Nature. 1990 Mar 1;344(6261):70-2. PMID:1968231 doi:http://dx.doi.org/10.1038/344070a0
↑ Hayashi T, Takahashi T, Motoya S, Ishida T, Itoh F, Adachi M, Hinoda Y, Imai K. MUC1 mucin core protein binds to the domain 1 of ICAM-1. Digestion. 2001;63 Suppl 1:87-92. PMID:11173916
↑ van Buul JD, Allingham MJ, Samson T, Meller J, Boulter E, Garcia-Mata R, Burridge K. RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration. J Cell Biol. 2007 Sep 24;178(7):1279-93. Epub 2007 Sep 17. PMID:17875742 doi:10.1083/jcb.200612053
↑ Xiao C, Bator-Kelly CM, Rieder E, Chipman PR, Craig A, Kuhn RJ, Wimmer E, Rossmann MG. The crystal structure of coxsackievirus A21 and its interaction with ICAM-1. Structure. 2005 Jul;13(7):1019-33. PMID:16004874 doi:10.1016/j.str.2005.04.011

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z7z"

@@ Line 3: / Line 3: @@
 <SX load='1z7z' size='340' side='right' viewer='molstar' caption='[[1z7z]], [[Resolution|resolution]] 8.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z7z]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_coxsackievirus_a21 Human coxsackievirus a21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z7Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z7z]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_coxsackievirus_a21 Human coxsackievirus a21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z7Z FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iam|1iam]], [[1z7s|1z7s]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iam|1iam]], [[1z7s|1z7s]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7z OCA], [http://pdbe.org/1z7z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z7z RCSB], [http://www.ebi.ac.uk/pdbsum/1z7z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7z ProSAT]</span></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=1z7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7z OCA], [https://pdbe.org/1z7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z7z RCSB], [https://www.ebi.ac.uk/pdbsum/1z7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7z ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ICAM1_HUMAN ICAM1_HUMAN]] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus.<ref>PMID:2538243</ref> <ref>PMID:1968231</ref> <ref>PMID:11173916</ref> <ref>PMID:17875742</ref>
+[[https://www.uniprot.org/uniprot/ICAM1_HUMAN ICAM1_HUMAN]] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus.<ref>PMID:2538243</ref> <ref>PMID:1968231</ref> <ref>PMID:11173916</ref> <ref>PMID:17875742</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
 *[[Intercellular adhesion molecule|Intercellular adhesion molecule]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>

1z7z

From Proteopedia

Revision as of 16:58, 20 October 2021

Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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