4egt

Crystal structure of major capsid protein P domain from rabbit hemorrhagic disease virusCrystal structure of major capsid protein P domain from rabbit hemorrhagic disease virus

Structural highlights 4egt is a 2 chain structure with sequence from Rabbit hemorrhagic disease virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3HNQ2_RHDV 3C-like protease processes the polyprotein: 3CLpro-RdRp (p72) is first released by autocleavage, then all other proteins are cleaved.[ARBA:ARBA00003176] Capsid protein VP60 self assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. Attaches virion to target cells by binding histo-blood group antigens, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm.[ARBA:ARBA00024666] NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.[ARBA:ARBA00025124] Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation.[ARBA:ARBA00025359] See Also Virus coat proteins 3D structures

spinqualitylabelsall models 4egt, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image