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PDBsum entry 2v4x
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Viral protein
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PDB id
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2v4x
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References listed in PDB file
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Key reference
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Title
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Structure of the capsid amino-Terminal domain from the betaretrovirus, Jaagsiekte sheep retrovirus.
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Authors
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G.B.Mortuza,
D.C.Goldstone,
C.Pashley,
L.F.Haire,
M.Palmarini,
W.R.Taylor,
J.P.Stoye,
I.A.Taylor.
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Ref.
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J Mol Biol, 2009,
386,
1179-1192.
[DOI no: ]
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PubMed id
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Abstract
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Jaagsiekte sheep retrovirus is a betaretrovirus and the causative agent of
pulmonary adenocarcinoma, a transmissible lung tumour of sheep. Here we report
the crystal structure of the capsid amino-terminal domain and examine the
self-association properties of Jaagsiekte sheep retrovirus capsid. We find that
the structure is remarkably similar to the amino-terminal domain of the
alpharetrovirus, avian leukosis virus, revealing a previously undetected
evolutionary similarity. Examination of capsid self-association suggests a mode
of assembly not driven by the strong capsid carboxy-terminal domain interactions
that characterise capsid assembly in the lentiviruses. Based on these data, we
propose this structure provides a model for the capsid of betaretroviruses
including the HML-2 family of endogenous human betaretroviruses.
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Figure 1.
Fig. 1. Crystal structure of the N-terminal domain of the
JSRV capsid. (a) A cartoon representation of the JSRV capsid
N-terminal domain, α-helices and β-strands are numbered. (b)
Cartoon representation of JSRV-NtD oriented at 90° to (a),
highlighting the α4–α6 loop.
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Figure 3.
Fig. 3. Ribbon view of α4 in the capsid N-terminal domains
of JSRV (a), RSV (b), HIV (c), MLV (d) and HTLV (e). The
functionally important arginine is indicated in each panel.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2009,
386,
1179-1192)
copyright 2009.
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