1fp0

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Borden, K.L.B.]]
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[[Category: Borden, K L.B.]]
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[[Category: Capili, A.D.]]
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[[Category: Capili, A D.]]
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[[Category: III, F.J.Rauscher.]]
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[[Category: III, F J.Rauscher.]]
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[[Category: Schultz, D.C.]]
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[[Category: Schultz, D C.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: c3hc4 type zinc binding domain]]
[[Category: c3hc4 type zinc binding domain]]
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[[Category: phd domain]]
[[Category: phd domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:48:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:05 2008''

Revision as of 10:41, 21 February 2008


1fp0

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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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