2V4X

Crystal Structure of Jaagsiekte Sheep Retrovirus Capsid N-terminal domain

Summary for 2V4X

• Entry DOI: 10.2210/pdb2v4x/pdb
• Descriptor: CAPSID PROTEIN P27 (2 entities in total)
• Functional Keywords: capsid, virion, retrovirus, zinc-finger, metal-binding, capsid protein, structural protein, viral nucleoprotein, viral matrix protein, viral protein
• Biological source: JAAGSIEKTE SHEEP RETROVIRUS
• Total number of polymer chains: 1
• Total formula weight: 16119.74

Authors

Mortuza, G.B.,Goldstone, D.C.,Pashley, C.,Haire, L.F.,Palmarini, M.,Taylor, W.R.,Stoye, J.P.,Taylor, I.A. (deposition date: 2008-09-30, release date: 2008-11-25, Last modification date: 2024-11-13)

Primary citation

Mortuza, G.B.,Goldstone, D.C.,Pashley, C.,Haire, L.F.,Palmarini, M.,Taylor, W.R.,Stoye, J.P.,Taylor, I.A.
Structure of the Capsid Amino-Terminal Domain from the Betaretrovirus, Jaagsiekte Sheep Retrovirus.
J.Mol.Biol., 386:1179-, 2009

PubMed Abstract: 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.

PubMed: 19007792
DOI: 10.1016/J.JMB.2008.10.066

Experimental method

X-RAY DIFFRACTION (1.5 Å)