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PDBsum entry 6y9v
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Viral protein
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PDB id
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6y9v
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Contents |
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146 a.a.
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(+ 2 more)
220 a.a.
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164 a.a.
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74 a.a.
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References listed in PDB file
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Key reference
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Title
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Intrinsic curvature of the HIV-1 ca hexamer underlies capsid topology and interaction with cyclophilin a.
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Authors
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T.Ni,
S.Gerard,
G.Zhao,
K.Dent,
J.Ning,
J.Zhou,
J.Shi,
J.Anderson-Daniels,
W.Li,
S.Jang,
A.N.Engelman,
C.Aiken,
P.Zhang.
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Ref.
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Nat Struct Mol Biol, 2020,
27,
855-862.
[DOI no: ]
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PubMed id
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Abstract
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The mature retrovirus capsid consists of a variably curved lattice of capsid
protein (CA) hexamers and pentamers. High-resolution structures of the curved
assembly, or in complex with host factors, have not been available. By devising
cryo-EM methodologies for exceedingly flexible and pleomorphic assemblies, we
have determined cryo-EM structures of apo-CA hexamers and in complex with
cyclophilin A (CypA) at near-atomic resolutions. The CA hexamers are
intrinsically curved, flexible and asymmetric, revealing the capsomere and not
the previously touted dimer or trimer interfaces as the key contributor to
capsid curvature. CypA recognizes specific geometries of the curved lattice,
simultaneously interacting with three CA protomers from adjacent hexamers via
two noncanonical interfaces, thus stabilizing the capsid. By determining
multiple structures from various helical symmetries, we further revealed the
essential plasticity of the CA molecule, which allows formation of continuously
curved conical capsids and the mechanism of capsid pattern sensing by CypA.
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