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Hepatitis B Capsid Protein with an N-terminal extension modelled into 8.9 A data.Hepatitis B Capsid Protein with an N-terminal extension modelled into 8.9 A data.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHepatitis B core (HBc) particles have been extensively exploited as carriers for foreign immunological epitopes in the development of multicomponent vaccines and diagnostic reagents. Crystals of the T = 4 HBc particle were grown in PEG 20,000, ammonium sulfate and various types of alcohols. A temperature jump from 277 or 283 to 290 K was found to enhance crystal growth. A crystal grown using MPD as a cryoprotectant diffracted X-rays to 7.7 A resolution and data were collected to 99.6% completeness at 8.9 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 352.3, b = 465.5, c = 645.0 A. The electron-density map reveals a protrusion that is consistent with the N-terminus extending out from the surface of the capsid. The structure presented here supports the idea that N-terminal insertions can be exploited in the development of diagnostic reagents, multicomponent vaccines and delivery vehicles into mammalian cells. Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension.,Tan WS, McNae IW, Ho KL, Walkinshaw MD Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):642-7. Epub 2007 Jul 21. PMID:17671358[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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