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5znf

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(New page: 200px<br /> <applet load="5znf" size="450" color="white" frame="true" align="right" spinBox="true" caption="5znf" /> '''ALTERNATING ZINC FINGERS IN THE HUMAN MALE ...)
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Revision as of 21:45, 12 November 2007


5znf

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ALTERNATING ZINC FINGERS IN THE HUMAN MALE ASSOCIATED PROTEIN ZFY: 2D NMR STRUCTURE OF AN EVEN FINGER AND IMPLICATIONS FOR "JUMPING-LINKER" DNA RECOGNITION

Contents

Overview

ZFY, a sex-related Zn-finger protein encoded by the human Y chromosome, is, distinguished from the general class of Zn-finger proteins by the presence, of a two-finger repeat. Whereas odd-numbered domains and linkers fit a, general consensus, even-numbered domains and linkers exhibit systematic, differences. Because this alternation may have fundamental implications, for the mechanism of protein-DNA recognition, we have undertaken, biochemical and structural studies of fragments of ZFY. We describe here, the solution structure of a representative nonconsensus (even-numbered) Zn, finger based on 2D NMR studies of a 30-residue peptide. Structural, modeling by distance geometry and simulated annealing (DG/SA) demonstrates, that this peptide folds as a miniglobular domain containing a C-terminal, beta--hairpin and N-terminal alpha-helix (beta beta alpha motif). These, features are similar to (but not identical with) those previously, described in consensus-type Zn fingers (derived from ADR1 and Xfin); the, similarities suggest that even and odd ZFY domains bind DNA by a common, mechanism. A model of the protein-DNA complex (designated the, "jumping-linker" model) is presented and discussed in terms of the ZFY, two-finger repeat. In this model every other linker is proposed to cross, the minor groove by means of a putative finger/linker submotif, HX4HX3-hydrophobic residue-X3. Analogous use of a hydrophobic residue in a, linker that spans the minor groove has recently been described in, crystallographic and 3D NMR studies of homeodomain-DNA complexes. The, proposed model of ZFY is supported in part by the hydroxyl radical, footprint of the TFIIIA-DNA complex [Churchill, M.E.A., Tullius, T.D., &, Klug, A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5528-5532].

Disease

Known disease associated with this structure: Spastic paraplegia 33 OMIM:[610243]

About this Structure

5ZNF is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for "jumping-linker" DNA recognition., Kochoyan M, Havel TF, Nguyen DT, Dahl CE, Keutmann HT, Weiss MA, Biochemistry. 1991 Apr 9;30(14):3371-86. PMID:1849423

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