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PDBsum entry 4cyc

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Top Page protein dna_rna Protein-protein interface(s) links
Transcription PDB id
4cyc
Contents
Protein chains
66 a.a.
58 a.a.
DNA/RNA
Waters ×68

References listed in PDB file
Key reference
Title A flexible extension of the drosophila ultrabithorax homeodomain defines a novel hox/pbc interaction mode.
Authors N.Foos, C.Maurel-Zaffran, M.J.Maté, R.Vincentelli, M.Hainaut, H.Berenger, J.Pradel, A.J.Saurin, M.Ortiz-Lombardía, Y.Graba.
Ref. Structure, 2015, 23, 270-279. [DOI no: 10.1016/j.str.2014.12.011]
PubMed id 25651060
Abstract
The patterning function of Hox proteins relies on assembling protein complexes with PBC proteins, which often involves a protein motif found in most Hox proteins, the so-called Hexapeptide (HX). Hox/PBC complexes likely gained functional diversity by acquiring additional modes of interaction. Here, we structurally characterize the first HX alternative interaction mode based on the paralogue-specific UbdA motif and further functionally validate structure-based predictions. The UbdA motif folds as a flexible extension of the homeodomain recognition helix and defines Hox/PBC contacts that occur, compared with those mediated by the HX motif, on the opposing side of the DNA double helix. This provides a new molecular facet to Hox/PBC complex assembly and suggests possible mechanisms for the diversification of Hox protein function.
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