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Crystal structure of Human enterovirus 71Crystal structure of Human enterovirus 71
Structural highlights
Function[A9X4C2_9ENTO] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047] Publication Abstract from PubMedEnterovirus 71 is a picornavirus associated with fatal neurological illness in infants and young children. Here, we report the crystal structure of enterovirus 71 and show that, unlike in other enteroviruses, the "pocket factor," a small molecule that stabilizes the virus, is partly exposed on the floor of the canyon. Thus, the structure of antiviral compounds may require a hydrophilic head group designed to interact with residues at the entrance of the pocket. Crystal Structure of Human Enterovirus 71.,Plevka P, Perera R, Cardosa J, Kuhn RJ, Rossmann MG Science. 2012 Mar 1. PMID:22383808[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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