2j12

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[[Image:2j12.gif|left|200px]]<br /><applet load="2j12" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j12, resolution 1.50&Aring;" />
 
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'''AD37 FIBRE HEAD IN COMPLEX WITH CAR D1'''<br />
 
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==Overview==
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==Ad37 fibre head in complex with CAR D1==
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Adenovirus fibers from most serotypes bind the D1 domain of coxsackie and, adenovirus receptor (CAR), although the binding residues are not strictly, conserved. To understand this further, we determined the crystal, structures of canine adenovirus serotype 2 (CAV-2) and the human, adenovirus serotype 37 (HAd37) in complex with human CAR D1 at 2.3 and, 1.5A resolution, respectively. Structure comparison with the HAd12 fiber, head-CAR D1 complex showed that the overall topology of the interaction is, conserved but that the interfaces differ in number and identity of, interacting residues, shape complementarity, and degree of conformational, adaptation. Using surface plasmon resonance, we characterized the binding, affinity to CAR D1 of wild type and mutant CAV-2 and HAd37 fiber heads. We, found that CAV-2 has the highest affinity but fewest direct interactions, with the reverse being true for HAd37. Moreover, we found that conserved, interactions can have a minor contribution, whereas serotype-specific, interactions can be essential. These results are discussed in the light of, virus evolution and design of adenovirus vectors for gene transfer.
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<StructureSection load='2j12' size='340' side='right'caption='[[2j12]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2j12]] 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_D37 Human adenovirus D37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J12 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j12 OCA], [https://pdbe.org/2j12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j12 RCSB], [https://www.ebi.ac.uk/pdbsum/2j12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j12 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q80S15_9ADEN Q80S15_9ADEN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j1/2j12_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2j12 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Adenovirus fibers from most serotypes bind the D1 domain of coxsackie and adenovirus receptor (CAR), although the binding residues are not strictly conserved. To understand this further, we determined the crystal structures of canine adenovirus serotype 2 (CAV-2) and the human adenovirus serotype 37 (HAd37) in complex with human CAR D1 at 2.3 and 1.5A resolution, respectively. Structure comparison with the HAd12 fiber head-CAR D1 complex showed that the overall topology of the interaction is conserved but that the interfaces differ in number and identity of interacting residues, shape complementarity, and degree of conformational adaptation. Using surface plasmon resonance, we characterized the binding affinity to CAR D1 of wild type and mutant CAV-2 and HAd37 fiber heads. We found that CAV-2 has the highest affinity but fewest direct interactions, with the reverse being true for HAd37. Moreover, we found that conserved interactions can have a minor contribution, whereas serotype-specific interactions can be essential. These results are discussed in the light of virus evolution and design of adenovirus vectors for gene transfer.
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==Disease==
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Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor.,Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S J Biol Chem. 2006 Nov 3;281(44):33704-16. Epub 2006 Aug 21. PMID:16923808<ref>PMID:16923808</ref>
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Known diseases associated with this structure: Adrenocortical tumor, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Carney complex, type 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Myxoma, intracardiac OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Pigmented adrenocortical disease, primary, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Spastic paraplegia-7 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602783 602783]], Thyroid carcinoma, papillary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2J12 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_adenovirus_type_49 Human adenovirus type 49] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J12 OCA].
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</div>
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<div class="pdbe-citations 2j12" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor., Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S, J Biol Chem. 2006 Nov 3;281(44):33704-16. Epub 2006 Aug 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16923808 16923808]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Human adenovirus type 49]]
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[[Category: Human adenovirus D37]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Billet, O.]]
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[[Category: Billet O]]
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[[Category: Cusac, S.]]
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[[Category: Cusack S]]
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[[Category: Kremer, E.J.]]
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[[Category: Kremer EJ]]
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[[Category: Lortat-Jacob, H.]]
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[[Category: Lortat-Jacob H]]
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[[Category: Seiradake, E.]]
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[[Category: Seiradake E]]
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[[Category: CA]]
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[[Category: ad37]]
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[[Category: adenovirus]]
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[[Category: alternative splicing]]
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[[Category: car]]
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[[Category: cell adhesion]]
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[[Category: complex]]
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[[Category: coxsackievirus]]
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[[Category: glycoprotein]]
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[[Category: had37]]
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[[Category: host-virus interaction]]
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[[Category: immunoglobulin domain]]
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[[Category: lipoprotein]]
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[[Category: membrane]]
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[[Category: palmitate]]
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[[Category: phosphorylation]]
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[[Category: receptor]]
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[[Category: tight junction]]
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[[Category: transmembrane]]
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[[Category: viral protein/receptor complex]]
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[[Category: x-ray]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:40:25 2008''
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Current revision

Ad37 fibre head in complex with CAR D1

PDB ID 2j12

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