2bl6
From Proteopedia
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SOLUTION STRUCTURE OF THE ZN COMPLEX OF EIAV NCP11(22-58) PEPTIDE, INCLUDING TWO CCHC ZN-BINDING MOTIFS.
Overview
Lentiviral nucleocapsid proteins are a class of multifunctional proteins, that play an essential role in RNA packaging and viral infectivity. They, contain two CX(2)CX(4)HX(4)C zinc binding motifs connected by a basic, linker of variable length. The 3D structure of a 37-aa peptide, corresponding to sequence 22-58 from lentiviral EIAV nucleocapsid protein, NCp11, complexed with zinc, has been determined by 2D (1)H 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, Omega-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.
About this Structure
2BL6 is a Single protein structure of sequence from [1] with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural features in EIAV NCp11: a lentivirus nucleocapsid protein with a short linker., Amodeo P, Castiglione Morelli MA, Ostuni A, Battistuzzi G, Bavoso A, Biochemistry. 2006 May 2;45(17):5517-26. PMID:16634633
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