PMID- 15386017
OWN - NLM
STAT- MEDLINE
DCOM- 20041005
LR  - 20041126
IS  - 1476-4687 (Electronic)
IS  - 0028-0836 (Linking)
VI  - 431
IP  - 7007
DP  - 2004 Sep 23
TI  - High-resolution structure of a retroviral capsid hexameric amino-terminal domain.
PG  - 481-5
AB  - Retroviruses are the aetiological agents of a range of human diseases including 
      AIDS and T-cell leukaemias. They follow complex life cycles, which are still only 
      partly understood at the molecular level. Maturation of newly formed retroviral 
      particles is an essential step in production of infectious virions, and requires 
      proteolytic cleavage of Gag polyproteins in the immature particle to form the 
      matrix, capsid and nucleocapsid proteins present in the mature virion. Capsid 
      proteins associate to form a dense viral core that may be spherical, cylindrical 
      or conical depending on the genus of the virus. Nonetheless, these assemblies all 
      appear to be composed of a lattice formed from hexagonal rings, each containing 
      six capsid monomers. Here, we describe the X-ray structure of an individual 
      hexagonal assembly from N-tropic murine leukaemia virus (N-MLV). The interface 
      between capsid monomers is generally polar, consistent with weak interactions 
      within the hexamer. Similar architectures are probably crucial for the regulation 
      of capsid assembly and disassembly in all retroviruses. Together, these 
      observations provide new insights into retroviral uncoating and how cellular 
      restriction factors may interfere with viral replication.
FAU - Mortuza, Gulnahar B
AU  - Mortuza GB
AD  - Division of Protein Structure, National Institute for Medical Research, The 
      Ridgeway, Mill Hill, London NW7 1AA, UK.
FAU - Haire, Lesley F
AU  - Haire LF
FAU - Stevens, Anthony
AU  - Stevens A
FAU - Smerdon, Stephen J
AU  - Smerdon SJ
FAU - Stoye, Jonathan P
AU  - Stoye JP
FAU - Taylor, Ian A
AU  - Taylor IA
LA  - eng
PT  - Journal Article
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Capsid Proteins)
SB  - IM
EIN - Nature. 2004 Oct 21;431(7011):1017
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Capsid/chemistry
MH  - Capsid Proteins/*chemistry
MH  - Crystallography, X-Ray
MH  - Leukemia Virus, Murine/*chemistry
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Structure, Quaternary
MH  - Protein Structure, Tertiary
MH  - Virus Assembly
EDAT- 2004/09/24 05:00
MHDA- 2004/10/06 09:00
CRDT- 2004/09/24 05:00
PHST- 2004/07/07 00:00 [received]
PHST- 2004/08/05 00:00 [accepted]
PHST- 2004/09/24 05:00 [pubmed]
PHST- 2004/10/06 09:00 [medline]
PHST- 2004/09/24 05:00 [entrez]
AID - nature02915 [pii]
AID - 10.1038/nature02915 [doi]
PST - ppublish
SO  - Nature. 2004 Sep 23;431(7007):481-5. doi: 10.1038/nature02915.