3j3q

Atomic-level structure of the entire HIV-1 capsid

Loading... Status: waiting for Mol* initialization Structural highlights 3j3q is a 1356 chain structure with sequence from Human immunodeficiency virus 1. This structure supersedes the now removed PDB entries 1vu4, 1vu5, 1vu6, 1vu7, 1vu8, 1vu9, 1vua, 1vuc, 1vud, 1vue, 1vuf, 1vug, 1vuh, 1vui, 1vuj, 1vuk, 1vul, 1vum, 1vun, 1vuo, 1vup, 1vuq, 1vur, 1vus and 1vut. The July 2013 RCSB PDB Molecule of the Month feature on HIV Capsid by David Goodsell is 10.2210/rcsb_pdb/mom_2013_7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q79791_9HIV1 Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).[SAAS:SAAS000071_004_008806] Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS000071_004_011858] Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat proteins 3D structures

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