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==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.

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==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Borden, K.L.B.]]

[[Category: Borden, K L.B.]]

[[Category: Capili, A.D.]]

[[Category: Capili, A D.]]

[[Category: III, F.J.Rauscher.]]

[[Category: III, F J.Rauscher.]]

[[Category: Schultz, D.C.]]

[[Category: Schultz, D C.]]

[[Category: ZN]]

[[Category: c3hc4 type zinc binding domain]]

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[[Category: phd domain]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Plant homeodomain (PHD) domains are found in &gt;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.
+Plant homeodomain (PHD) domains are found in &gt;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==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Borden, K.L.B.]]
+[[Category: Borden, K L.B.]]
-[[Category: Capili, A.D.]]
+[[Category: Capili, A D.]]
-[[Category: III, F.J.Rauscher.]]
+[[Category: III, F J.Rauscher.]]
-[[Category: Schultz, D.C.]]
+[[Category: Schultz, D C.]]
 [[Category: ZN]]
 [[Category: c3hc4 type zinc binding domain]]
@@ Line 22: / Line 22: @@
 [[Category: phd domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:48:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:05 2008''