1x4s

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Solution structure of zinc finger HIT domain in protein FON

Overview

The zinc finger HIT domain is a sequence motif found in many proteins, including thyroid hormone receptor interacting protein 3 (TRIP-3), which, is possibly involved in maturity-onset diabetes of the young (MODY). Novel, zinc finger motifs are suggested to play important roles in gene, regulation and chromatin remodeling. Here, we determined the, high-resolution solution structure of the zinc finger HIT domain in ZNHIT2, (protein FON) from Homo sapiens, by an NMR method based on 567 upper, distance limits derived from NOE intensities measured in three-dimensional, NOESY spectra. The structure yielded a backbone RMSD to the mean, coordinates of 0.19 A for the structured residues 12-48. The fold consists, of two consecutive antiparallel beta-sheets and two short C-terminal, helices packed against the second beta-sheet, and binds two zinc ions., Both zinc ions are coordinated tetrahedrally via a CCCC-CCHC motif to the, ligand residues of the zf-HIT domain in an interleaved manner. The, tertiary structure of the zinc finger HIT domain closely resembles the, folds of the B-box, RING finger, and PHD domains with a cross-brace zinc, coordination mode, but is distinct from them. The unique three-dimensional, structure of the zinc finger HIT domain revealed a novel zinc-binding, fold, as a new member of the treble clef domain family. On the basis of, the structural data, we discuss the possible functional roles of the zinc, finger HIT domain.

About this Structure

1X4S is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of the zinc finger HIT domain in protein FON., He F, Umehara T, Tsuda K, Inoue M, Kigawa T, Matsuda T, Yabuki T, Aoki M, Seki E, Terada T, Shirouzu M, Tanaka A, Sugano S, Muto Y, Yokoyama S, Protein Sci. 2007 Aug;16(8):1577-87. PMID:17656577

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