1vyi is a 1 chain structure with sequence from Viruses. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The phosphoprotein (P) of rabies virus binds the viral polymerase to the nucleoprotein (N)-RNA template for transcription and replication. By limited protease digestion we defined a monomeric C-terminal domain of P that can bind to N-RNA. The atomic structure of this domain was determined and previously described mutations that interfere with binding of P to N-RNA could now be interpreted. There appears to be two features involved in this activity situated at opposite surfaces of the molecule: a positively charged patch and a hydrophobic pocket with an exposed tryptophan side-chain. Other previously published work suggests a conformational change in P when it binds to N-RNA, which may imply the repositioning of two helices that would expose a hydrophobic groove for interaction with N. This domain of rabies virus P is structurally unrelated to the N-RNA binding domains of the phosphoproteins of Sendai and measles virus that are members of the same order of viruses, the non-segmented negative strand RNA viruses. The implications of this finding for the evolution of this virus group are discussed.
Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus.,Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RW J Mol Biol. 2004 Oct 29;343(4):819-31. PMID:15476803[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RW. Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus. J Mol Biol. 2004 Oct 29;343(4):819-31. PMID:15476803 doi:10.1016/j.jmb.2004.08.071
