1kac: Difference between revisions

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-{{Seed}}
-[[Image:1kac.png|left|200px]]
-<!--
+==KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR==
-The line below this paragraph, containing "STRUCTURE_1kac", creates the "Structure Box" on the page.
+<StructureSection load='1kac' size='340' side='right'caption='[[1kac]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1kac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_adenovirus_12 Human adenovirus 12]. 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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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>
-{{STRUCTURE_1kac|  PDB=1kac  |  SCENE=  }}
+</table>
+== Function ==
+[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).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ka/1kac_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kac ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR===
+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<ref>PMID:10567268</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_10567268}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1kac" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 10567268 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10567268}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Adenovirus]]
-KAC is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_adenovirus_12 Human adenovirus 12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAC OCA].
-==Reference==
-<ref group="xtra">PMID:10567268</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
 [[Category: Human adenovirus 12]]
-[[Category: Bewley, M C.]]
+[[Category: Large Structures]]
-[[Category: Flanagan, J M.]]
+[[Category: RCSB PDB Molecule of the Month]]
-[[Category: Freimuth, P.]]
+[[Category: Bewley MC]]
-[[Category: Springer, K.]]
+[[Category: Flanagan JM]]
-[[Category: Zhang, Y B.]]
+[[Category: Freimuth P]]
-[[Category: Adhesion protein receptor complex]]
+[[Category: Springer K]]
-[[Category: Viral protein/receptor complex]]
+[[Category: Zhang YB]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 03:59:15 2009''