1nc8

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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:57:11 2007''
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Revision as of 13:38, 30 October 2007


1nc8

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HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF THE MINIMAL ACTIVE DOMAIN OF THE HUMAN IMMUNODEFICIENCY VIRUS TYPE-2 NUCLEOCAPSID PROTEIN, 15 STRUCTURES

Overview

The retroviral nucleocapsid (NC) protein is a multifunctional protein, essential for RNA genome packaging and viral infectivity. The NC protein, NCp8, of the human immunodeficiency virus type-II (HIV-2) is a 49 amino, acid peptide containing two zinc fingers, of the type C-X2-C-X4-H-X4-C, connected by seven amino acid residues, called the "basic amino acid, cluster." It has been shown that the N-terminal zinc finger flanked by the, basic amino acid cluster is the minimal active domain for the specific, binding to viral RNA and other functions. However, the structure-activity, relationships of NCp8 have not been investigated in detail. In the present, study, the three-dimensional structure of a 29 amino acid peptide, including the minimal active domain (NCp8-fl), was determined by, ... [(full description)]

About this Structure

1NC8 is a [Single protein] structure of sequence from [Human immunodeficiency virus 1] with ZN as [ligand]. Structure known Active Site: ZNB. Full crystallographic information is available from [OCA].

Reference

High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein., Kodera Y, Sato K, Tsukahara T, Komatsu H, Maeda T, Kohno T, Biochemistry. 1998 Dec 22;37(51):17704-13. PMID:9922136

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