Lentiviral nucleocapsid proteins are a class of multifunctional proteins that play an essential role in RNA packaging and viral infectivity. They contain two CX2CX4HX4C zinc binding motifs connected by a basic linker of variable length. The 3D structure of a 37-aa peptide corresponding to sequence 2258 from lentiviral EIAV nucleocapsid protein NCp11, complexed with zinc, has been determined by 2D H-1 NMR spectroscopy, simulated annealing, and molecular dynamics. The solution structure consists of two zinc binding domains held together by a five-residue basic linker Arg(38)-Ala-Pro-Lys-Val(42) that allows for spatial proximity between the two finger domains. Observed linker folding is stabilized by H bonded secondary structure elements, resulting in an Q-shaped central region, asymmetrically centered on the linker. The conformational differences and similarities with other NC zinc binding knuckles have been systematically analyzed. The two CCHC motifs, both characterized by a peculiar Pro-Gly sequence preceding the His residue, although preserving Zn-binding geometry and chirality of other known NC proteins, exhibit local fold differences both between each other and in comparison with other previously characterized retroviral CCHC motifs.
|Anno di pubblicazione:||2006|
|Titolo:||Structural features in EIAV NCp11: A lentivirus nucleocapsid protein with a short linker|
|Autori:||Amodeo P; Morelli MAC; Ostuni A; Battistuzzi G; Bavoso A|
|Appare nelle tipologie:||Articolo su rivista|
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