1FP0

SOLUTION STRUCTURE OF THE PHD DOMAIN FROM THE KAP-1 COREPRESSOR

Summary for 1FP0

• Entry DOI: 10.2210/pdb1fp0/pdb
• Descriptor: KAP-1 COREPRESSOR, ZINC ION (2 entities in total)
• Functional Keywords: phd domain, c3hc4 type zinc binding domain, nmr-structure, transcription
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 10070.02

Authors

Capili, A.D.,Schultz, D.C.,Rauscher III, F.J.,Borden, K.L.B. (deposition date: 2000-08-29, release date: 2001-01-24, Last modification date: 2024-05-22)

Primary citation

Capili, A.D.,Schultz, D.C.,RauscherIII, F.J.,Borden, K.L.
Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains.
EMBO J., 20:165-177, 2001

PubMed Abstract: 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.

PubMed: 11226167
DOI: 10.1093/emboj/20.1.165

Experimental method

SOLUTION NMR