1kac

From Proteopedia

(Difference between revisions)

Revision as of 06:51, 11 August 2021

KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR

Structural highlights

1kac is a 2 chain structure with sequence from Ade12 and Human. The December 2010 RCSB PDB Molecule of the Month feature on Adenovirus by David Goodsell is 10.2210/rcsb_pdb/mom_2010_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1nob
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPIKE_ADE12] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CXCAR to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface (By similarity). [CXAR_HUMAN] Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Binding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors.

Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR.,Bewley MC, Springer K, Zhang YB, Freimuth P, Flanagan JM Science. 1999 Nov 19;286(5444):1579-83. PMID:10567268^[5]

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

References

↑ Tomko RP, Xu R, Philipson L. HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3352-6. PMID:9096397
↑ Cohen CJ, Shieh JT, Pickles RJ, Okegawa T, Hsieh JT, Bergelson JM. The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15191-6. Epub 2001 Dec 4. PMID:11734628 doi:10.1073/pnas.261452898
↑ Walters RW, Freimuth P, Moninger TO, Ganske I, Zabner J, Welsh MJ. Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape. Cell. 2002 Sep 20;110(6):789-99. PMID:12297051
↑ Zen K, Liu Y, McCall IC, Wu T, Lee W, Babbin BA, Nusrat A, Parkos CA. Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils. Mol Biol Cell. 2005 Jun;16(6):2694-703. Epub 2005 Mar 30. PMID:15800062 doi:E05-01-0036
↑ Bewley MC, Springer K, Zhang YB, Freimuth P, Flanagan JM. Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR. Science. 1999 Nov 19;286(5444):1579-83. PMID:10567268

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1kac' size='340' side='right'caption='[[1kac]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kac]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade12 Ade12] and [http://en.wikipedia.org/wiki/Human Human]. The December 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adenovirus''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_12 10.2210/rcsb_pdb/mom_2010_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KAC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ade12 Ade12] and [https://en.wikipedia.org/wiki/Human Human]. The December 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adenovirus''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_12 10.2210/rcsb_pdb/mom_2010_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KAC FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nob|1nob]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nob|1nob]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kac OCA], [http://pdbe.org/1kac PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kac RCSB], [http://www.ebi.ac.uk/pdbsum/1kac PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kac 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=1kac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kac OCA], [https://pdbe.org/1kac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kac RCSB], [https://www.ebi.ac.uk/pdbsum/1kac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kac ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SPIKE_ADE12 SPIKE_ADE12]] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CXCAR to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface (By similarity). [[http://www.uniprot.org/uniprot/CXAR_HUMAN CXAR_HUMAN]] Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN.<ref>PMID:9096397</ref> <ref>PMID:11734628</ref> <ref>PMID:12297051</ref> <ref>PMID:15800062</ref>
+[[https://www.uniprot.org/uniprot/SPIKE_ADE12 SPIKE_ADE12]] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CXCAR to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface (By similarity). [[https://www.uniprot.org/uniprot/CXAR_HUMAN CXAR_HUMAN]] Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN.<ref>PMID:9096397</ref> <ref>PMID:11734628</ref> <ref>PMID:12297051</ref> <ref>PMID:15800062</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1kac

From Proteopedia

Revision as of 06:51, 11 August 2021

KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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