1SVP

SINDBIS VIRUS CAPSID PROTEIN

Summary for 1SVP

• Entry DOI: 10.2210/pdb1svp/pdb
• Descriptor: SINDBIS VIRUS CAPSID PROTEIN (2 entities in total)
• Functional Keywords: sindbis virus capsid protein, chymotrypsin-like serine, mutant, coat protein, viral protein
• Biological source: Sindbis virus
• Cellular location: Capsid protein: Virion (By similarity). p62: Virion membrane; Single-pass type I membrane protein (By similarity). E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein (By similarity). 6K protein: Host cell membrane; Multi-pass membrane protein (By similarity): P03316
• Total number of polymer chains: 2
• Total formula weight: 35121.68

Authors

Lee, S.,Rossmann, M.G. (deposition date: 1996-03-22, release date: 1996-08-17, Last modification date: 2024-02-14)

Primary citation

Lee, S.,Owen, K.E.,Choi, H.K.,Lee, H.,Lu, G.,Wengler, G.,Brown, D.T.,Rossmann, M.G.,Kuhn, R.J.
Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly.
Structure, 4:531-541, 1996

PubMed Abstract: Many enveloped viruses exit cells by budding from the plasma membrane. The driving force for budding is the interaction of an inner protein nucleocapsid core with transmembrane glycoprotein spikes. The molecular details of this process are ill defined. Alphaviruses, such as Sindbis virus (SINV) and Semliki Forest virus (SFV), represent some of the simplest enveloped viruses and have been well characterized by structural, genetic and biochemical techniques. Although a high-resolution structure of an alphavirus has not yet been attained, cryo-electron microscopy (cryo-EM) has been used to show the multilayer organization at 25 A resolution. In addition, atomic resolution studies are available of the C-terminal domain of the nucleocapsid protein and this has been modeled into the cryo-EM density.

PubMed: 8736552
DOI: 10.1016/S0969-2126(96)00059-7

Experimental method

X-RAY DIFFRACTION (2 Å)