Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.

The Journal of Biological Chemistry
Ta-Hsien LinDer-Lii M Tzou

Abstract

This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa, containing this domain in which cysteines 71 and 72 were replaced with alanine, was constructed to prevent self-assembly due to intermolecular disulfide bonds between these two cysteines. The soluble eA27L-aa protein forms an oligomer resembling that of A27L on vaccinia virions. Heteronuclear correlation NMR spectroscopy was carried out on eA27L-aa in the presence or absence of urea to determine backbone resonance assignments. Chemical shift index (CSI) propensity analysis showed that eA27L-aa has two distinct structural domains, a relatively flexible 22-amino acid random coil in the N-terminal region and a fairly rigid alpha-helix structure in the remainder of the structure. Binding interaction studies using isothermal titration calorimetry suggest that a 12-amino acid lysine/arginine-rich segment in the N-terminal region is responsible for glycosaminoglycan binding. The rigid alpha-helix portion of eA27L-aa is probably involved in the intrinsic self-assembly, and CSI propensity analysis suggests that region N37-E49, with a residual alpha-helix...Continue Reading

References

Aug 1, 1995·Journal of Virology·D RodríguezJ R Rodríguez
Jan 1, 1994·Methods in Enzymology·D S Wishart, B D Sykes
Sep 1, 1996·Protein Science : a Publication of the Protein Society·Y Wang, D Shortle
Jan 1, 1997·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·L E Kay
Jul 1, 1997·Archives of Biochemistry and Biophysics·J R FrommR J Linhardt
Oct 29, 1997·Archives of Biochemistry and Biophysics·J R FrommR J Linhardt
Aug 6, 1998·Journal of Biomolecular NMR·A T Alexandrescu, K Rathgeb-Szabo
Mar 7, 2001·Science·M J RootP S Kim

❮ Previous
Next ❯

Citations

Jul 22, 2005·Journal of Biomolecular NMR·Feng-I ChuDer-Lii M Tzou
Oct 7, 2003·Annual Review of Microbiology·Geoffrey L SmithMansun Law
Jan 21, 2004·Journal of Molecular Recognition : JMR·Matthew J Cliff, John E Ladbury
Aug 22, 2007·Cellular Microbiology·Grazyna KochanMariano Esteban
Sep 2, 2016·Advanced Healthcare Materials·Benjamin ZiemRainer Haag

❮ Previous
Next ❯

Related Concepts

Related Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

Cajal Bodies & Gems

Cajal bodies or coiled bodies are dense foci of coilin protein. Gemini of Cajal bodies, or gems, are microscopically similar to Cajal bodies. It is believed that Cajal bodies play important roles in RNA processing while gems assist the Cajal bodies. Find the latest research on Cajal bodies and gems here.