4v86: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4v86]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Adeno-associated_virus_-_6 Adeno-associated virus - 6]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu0 1vu0], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu1 1vu1] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3tsx 3tsx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V86 FirstGlance]. <br>
-</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=4v86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v86 OCA], [https://pdbe.org/4v86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v86 RCSB], [https://www.ebi.ac.uk/pdbsum/4v86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v86 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.003&#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=4v86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v86 OCA], [https://pdbe.org/4v86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v86 RCSB], [https://www.ebi.ac.uk/pdbsum/4v86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v86 ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/O56137_9VIRU O56137_9VIRU]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Crystal structures of the AAV-6 capsid at 3A reveal a subunit fold homologous to other parvoviruses with greatest differences in two external loops. The electrostatic potential suggests that receptor-attachment is mediated by four residues: Arg(576), Lys(493), Lys(459) and Lys(531), defining a positively charged region curving up from the valley between adjacent spikes. It overlaps only partially with the receptor-binding site of AAV-2, and the residues endowing the electrostatic character are not homologous. Mutational substitution of each residue decreases heparin affinity, particularly Lys(531) and Lys(459). Neither is conserved among heparin-binding serotypes, indicating that diverse modes of receptor attachment have been selected in different serotypes. Surface topology and charge are also distinct at the shoulder of the spike, where linear epitopes for AAV-2's neutralizing monoclonal antibody A20 come together. Evolutionarily, selection of changed side-chain charge may have offered a conservative means to evade immune neutralization while preserving other essential functionality.
-Structure-function analysis of receptor-binding in adeno-associated virus serotype 6 (AAV-6).,Xie Q, Lerch TF, Meyer NL, Chapman MS Virology. 2011 Nov 10;420(1):10-9. Epub 2011 Sep 13. PMID:21917284<ref>PMID:21917284</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4v86" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>

4v86: Difference between revisions

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