1U7K

Structure of a hexameric N-terminal domain from murine leukemia virus capsid

Summary for 1U7K

• Entry DOI: 10.2210/pdb1u7k/pdb
• Descriptor: Gag polyprotein (2 entities in total)
• Functional Keywords: capsid, viral protein
• Biological source: AKR (endogenous) murine leukemia virus
• Cellular location: Gag polyprotein: Virion (By similarity). Matrix protein p15: Virion (Potential). Capsid protein p30: Virion (Potential). Nucleocapsid protein p10: Virion (Potential): P03336
• Total number of polymer chains: 6
• Total formula weight: 90026.49

Authors

Mortuza, G.B.,Haire, L.F.,Stevens, A.,Smerdon, S.J.,Stoye, J.P.,Taylor, I.A. (deposition date: 2004-08-04, release date: 2004-10-05, Last modification date: 2011-07-13)

Primary citation

Mortuza, G.B.,Haire, L.F.,Stevens, A.,Smerdon, S.J.,Stoye, J.P.,Taylor, I.A.
High-resolution structure of a retroviral capsid hexameric amino-terminal domain.
Nature, 431:481-485, 2004

PubMed Abstract: 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.

PubMed: 15386017
DOI: 10.1038/nature02915

Experimental method

X-RAY DIFFRACTION (1.85 Å)