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1fp0
From Proteopedia
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SOLUTION STRUCTURE OF THE PHD DOMAIN FROM THE KAP-1 COREPRESSOR
Overview
Plant homeodomain (PHD) domains are found in >400 eukaryotic proteins, many of which are transcriptional regulators. Naturally occurring point, mutations or deletions of this domain contribute to a variety of human, diseases, including ATRX syndrome, myeloid leukemias and autoimmune, dysfunction. Here we report the first structural characterization of a PHD, domain. Our studies reveal that the PHD domain from KAP-1 corepressor, binds zinc in a cross-brace topology between anti-parallel ss-strands, reminiscent of RING (really interesting new gene) domains. Using a, mutational analysis, we define the structural features required for, transcriptional repression by KAP-1 and explain naturally occurring, disease-causing mutations in PHD domains of other proteins. From a, comparison of this PHD structure with previously reported RING and LIM, (Lin11/Isl-1/Mec-3) structures, we infer sequence determinants that allow, discrimination among PHD, RING and LIM motifs.
About this Structure
1FP0 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 PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains., Capili AD, Schultz DC, RauscherIII FJ, Borden KL, EMBO J. 2001 Jan 15;20(1-2):165-77. PMID:11226167
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