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Publication Abstract from PubMed

A new protein expression vector design utilizing an N-terminal six-histidine tag and tobacco etch virus protease cleavage site upstream of the hepatitis C virus NS5A sequence has resulted in a more straightforward purification method and improved yields of purified NS5A domain I protein. High-resolution diffracting crystals of NS5A domain I (amino acids 33 to 202) [NS5A(33-202)] were obtained by using detergent additive crystallization screens, leading to the structure of a homodimer which is organized differently from that published previously (T. L. Tellinghuisen, J. Marcotrigiano, and C. M. Rice, Nature 435:374-379, 2005) yet is consistent with a membrane association model for NS5A. The monomer-monomer interface of NS5A(33-202) features an extensive buried surface area involving the most-highly conserved face of each monomer. The two alternate structural forms of domain I now available may be indicative of the multiple roles emerging for NS5A in viral RNA replication and viral particle assembly.

Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus.,Love RA, Brodsky O, Hickey MJ, Wells PA, Cronin CN J Virol. 2009 May;83(9):4395-403. Epub 2009 Feb 25. PMID:19244328^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.