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3j3q

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====
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<div style="background-color:yellow;" border="1" cellpadding="5">''Warning: this is a large structure, and loading might take a long time or not happen at all.''</div>
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<StructureSection load='3j3q' size='340' side='right' caption='[[3j3q]]' scene=''>
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== Atomic-level structure of the entire HIV-1 capsid ==
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<StructureSection load='3j3q-pdb-bundle1.pdb.gz' size='340' side='right' caption='[[3j3q]]' scene=''>
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== Structural highlights ==
== Structural highlights ==
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[[3j3q]] is a 1355 chain structure, available for rendering on Proteopedia in 25 parts.
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<table><tr><td colspan='2'>This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu4 1vu4], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu5 1vu5], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu6 1vu6], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu7 1vu7], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu8 1vu8], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vu9 1vu9], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vua 1vua], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vuc 1vuc], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vud 1vud], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vue 1vue], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vuf 1vuf], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vug 1vug], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vuh 1vuh], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vui 1vui], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vuj 1vuj], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vuk 1vuk], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vul 1vul], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vum 1vum], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vun 1vun], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vuo 1vuo], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vup 1vup], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vuq 1vuq], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vur 1vur], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vus 1vus] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vut 1vut]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol= FirstGlance]. <br>
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You may render each one of these parts individually by selecting here: <jmol><jmolMenu>
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</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=3j3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j3q RCSB], [http://www.ebi.ac.uk/pdbsum/3j3q PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Retroviral capsid proteins are conserved structurally but assemble into different morphologies. The mature human immunodeficiency virus-1 (HIV-1) capsid is best described by a 'fullerene cone' model, in which hexamers of the capsid protein are linked to form a hexagonal surface lattice that is closed by incorporating 12 capsid-protein pentamers. HIV-1 capsid protein contains an amino-terminal domain (NTD) comprising seven alpha-helices and a beta-hairpin, a carboxy-terminal domain (CTD) comprising four alpha-helices, and a flexible linker with a 310-helix connecting the two structural domains. Structures of the capsid-protein assembly units have been determined by X-ray crystallography; however, structural information regarding the assembled capsid and the contacts between the assembly units is incomplete. Here we report the cryo-electron microscopy structure of a tubular HIV-1 capsid-protein assembly at 8 A resolution and the three-dimensional structure of a native HIV-1 core by cryo-electron tomography. The structure of the tubular assembly shows, at the three-fold interface, a three-helix bundle with critical hydrophobic interactions. Mutagenesis studies confirm that hydrophobic residues in the centre of the three-helix bundle are crucial for capsid assembly and stability, and for viral infectivity. The cryo-electron-microscopy structures enable modelling by large-scale molecular dynamics simulation, resulting in all-atom models for the hexamer-of-hexamer and pentamer-of-hexamer elements as well as for the entire capsid. Incorporation of pentamers results in closer trimer contacts and induces acute surface curvature. The complete atomic HIV-1 capsid model provides a platform for further studies of capsid function and for targeted pharmacological intervention.
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Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics.,Zhao G, Perilla JR, Yufenyuy EL, Meng X, Chen B, Ning J, Ahn J, Gronenborn AM, Schulten K, Aiken C, Zhang P Nature. 2013 May 30;497(7451):643-6. doi: 10.1038/nature12162. PMID:23719463<ref>PMID:23719463</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>
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[[Category: Zhao, G]]
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[[Category: Z-disk]]
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[[Category: Zhang, P]]
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[[Category: Schulten, K.J]]
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[[Category: Perilla, J.R]]
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Revision as of 13:28, 1 September 2015

==

3j3q

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