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Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography
- Source :
- Science, Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩, Science, American Association for the Advancement of Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩
- Publication Year :
- 2015
- Publisher :
- HAL CCSD, 2015.
-
Abstract
- Retroviral capsids in their native form Capsid proteins of retroviruses form protective lattices around viral RNA molecules. The precise molecular details of how individual, full-length capsid proteins assemble to shield the viral genome; however, are not well understood. Obal et al. and Gres et al. now report high resolution crystal structures of the full length capsid proteins from Bovine Leukemia Virus and HIV-1, respectively. The two studies complement each other to reveal the dynamic nature of capsid protein assembly and of how individual capsid proteins interact in the lattice. The findings may have relevance for drug design. Science , this issue p. 95 ; see also p. 99
- Subjects :
- MESH: Mutation
Viral protein
Protein subunit
viruses
MESH: Protein Structure, Secondary
MESH: Amino Acid Sequence
Random hexamer
medicine.disease_cause
03 medical and health sciences
MESH: Leukemia Virus, Bovine
Retrovirus
Protein structure
medicine
[CHIM.CRIS]Chemical Sciences/Cristallography
MESH: Capsid
MESH: Animals
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]
Peptide sequence
MESH: Capsid Proteins
030304 developmental biology
0303 health sciences
Multidisciplinary
MESH: Molecular Sequence Data
biology
Bovine leukemia virus
MESH: Protein Multimerization
030302 biochemistry & molecular biology
biology.organism_classification
MESH: Crystallography, X-Ray
Virology
3. Good health
MESH: Cattle
Capsid
[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
Biophysics
Subjects
Details
- Language :
- English
- ISSN :
- 00368075 and 10959203
- Database :
- OpenAIRE
- Journal :
- Science, Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩, Science, American Association for the Advancement of Science, 2015, 349 (6243), pp.95-98. ⟨10.1126/science.aaa5182⟩
- Accession number :
- edsair.doi.dedup.....8cdf796db6cf18c981cf6f8d8ef88625