1fp0
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1fp0 |SIZE=350|CAPTION= <scene name='initialview01'>1fp0</scene> | |PDB= 1fp0 |SIZE=350|CAPTION= <scene name='initialview01'>1fp0</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fp0 OCA], [http://www.ebi.ac.uk/pdbsum/1fp0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fp0 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[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]] | [[Category: c3hc4 type zinc binding domain]] | ||
[[Category: nmr-structure]] | [[Category: nmr-structure]] | ||
[[Category: phd domain]] | [[Category: phd domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:18 2008'' |
Revision as of 17:27, 30 March 2008
| |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 20:27:18 2008
