1nc8
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(New page: 200px<br /> <applet load="1nc8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nc8" /> '''HIGH-RESOLUTION SOLUTION NMR STRUCTURE OF T...)
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Revision as of 19:13, 29 October 2007
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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 2] with ZN as [ligand]. 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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