Abstract:
:The structure of the dimeric C-terminal domain of the HIV-1 capsid protein (CA), recently determined by X-ray crystallography (Gamble et al. (1997)), has a notable resemblance to the structure of the hepatitis B virus (HBV) capsid protein (Cp) dimer, previously determined by cryo-electron microscopy (Conway et al. (1997), Böttcher et al. (1997)). In both proteins, dimerization is effected by formation of a four-helix bundle, whereby each subunit contributes a helix-loop-helix and most of the interaction between subunits is mediated by one pair of helices. These are the first two observations of a motif that is common to the capsid proteins of two enveloped viruses and quite distinct from the eight-stranded anti-parallel beta-barrel found in most other virus capsid proteins solved to date (Harrison et al. (1996)). Motivated by the structural resemblance, we have examined retroviral and HBV capsid protein sequences and found weak but significant similarities between them. These similarities further support an evolutionary relationship between these two virus families of great medical importance -- the hepadnaviruses (e.g. HBV) and retroviruses (e.g. HIV).
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zlotnick A,Stahl SJ,Wingfield PT,Conway JF,Cheng N,Steven ACdoi
10.1016/s0014-5793(98)00755-8subject
Has Abstractpub_date
1998-07-24 00:00:00pages
301-4issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00755-8journal_volume
431pub_type
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