3fqq | pdb_00003fqq
From Proteopedia
Crystal structure of a novel dimeric form of HCV NS5A domain I protein
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA 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. References
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