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2znf

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{{STRUCTURE_2znf| PDB=2znf | SCENE= }}
{{STRUCTURE_2znf| PDB=2znf | SCENE= }}
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'''HIGH-RESOLUTION STRUCTURE OF AN HIV ZINC FINGERLIKE DOMAIN VIA A NEW NMR-BASED DISTANCE GEOMETRY APPROACH'''
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===HIGH-RESOLUTION STRUCTURE OF AN HIV ZINC FINGERLIKE DOMAIN VIA A NEW NMR-BASED DISTANCE GEOMETRY APPROACH===
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==Overview==
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A new method is described for determining molecular structures from NMR data. The approach utilizes 2D NOESY back-calculations to generate simulated spectra for structures obtained from distance geometry (DG) computations. Comparison of experimental and back-calculated spectra, including analysis of cross-peak buildup and auto-peak decay with increasing mixing time, provides a quantitative measure of the consistence between the experimental data and generated structures and allows for use of tighter interproton distance constraints. For the first time, the "goodness" of the generated structures is evaluated on the basis of their consistence with the actual experimental data rather than on the basis of consistence with other generated structures. This method is applied to the structure determination of an 18-residue peptide with an amino acid sequence comprising the first zinc fingerlike domain from the gag protein p55 of HIV. This is the first structure determination to atomic resolution for a retroviral zinc fingerlike complex. The peptide [Zn(p55F1)] exhibits a novel folding pattern that includes type I and type II NH-S tight turns and is stabilized both by coordination of the three Cys and one His residues to zinc and by extensive internal hydrogen bonding. The backbone folding is significantly different from that of a "classical" DNA-binding zinc finger. Residues C(1)-F(2)-N(3)-C(4)-G(5)-K(6) fold in a manner virtually identical with the folding observed by X-ray crystallography for related residues in the iron domain of rubredoxin; superposition of all main-chain and Cys side-chain atoms of residues C(1)-K(6) of Zn(p55F1) onto residues C(6)-Y(11) and C(39)-V(44) of rubredoxin gives RMSDs of 0.46 and 0.35 A, respectively. The side chains of conservatively substituted Phe and Ile residues implicated in genomic RNA recognition form a hydrophobic patch on the peptide surface.
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(as it appears on PubMed at http://www.pubmed.gov), where 2105740 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2105740}}
==About this Structure==
==About this Structure==
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2ZNF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZNF OCA].
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2ZNF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZNF OCA].
==Reference==
==Reference==
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[[Category: Summers, M F.]]
[[Category: Summers, M F.]]
[[Category: Aids-related virus gag polyprotein]]
[[Category: Aids-related virus gag polyprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:14:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:22:08 2008''

Revision as of 14:22, 28 July 2008

Image:2znf.png

Template:STRUCTURE 2znf

HIGH-RESOLUTION STRUCTURE OF AN HIV ZINC FINGERLIKE DOMAIN VIA A NEW NMR-BASED DISTANCE GEOMETRY APPROACH

Template:ABSTRACT PUBMED 2105740

About this Structure

2ZNF is a Single protein structure of sequence from Human immunodeficiency virus 1. Full experimental information is available from OCA.

Reference

High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach., Summers MF, South TL, Kim B, Hare DR, Biochemistry. 1990 Jan 16;29(2):329-40. PMID:2105740

Page seeded by OCA on Mon Jul 28 17:22:08 2008

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