1KW4
Polyhomeotic SAM domain structure
Summary for 1KW4
Entry DOI | 10.2210/pdb1kw4/pdb |
Related | 1JI7 |
Descriptor | Polyhomeotic (2 entities in total) |
Functional Keywords | sam domain, polycomb group, polymer, dna binding protein |
Biological source | Drosophila melanogaster (fruit fly) |
Cellular location | Nucleus: P39769 |
Total number of polymer chains | 1 |
Total formula weight | 10319.45 |
Authors | Kim, C.A.,Gingery, M.,M Pilpa, R.,Bowie, J.U. (deposition date: 2002-01-28, release date: 2002-06-05, Last modification date: 2021-10-27) |
Primary citation | Kim, C.A.,Gingery, M.,Pilpa, R.M.,Bowie, J.U. The SAM domain of polyhomeotic forms a helical polymer. Nat.Struct.Biol., 9:453-457, 2002 Cited by PubMed Abstract: The polycomb group (PcG) proteins are important in the maintenance of stable repression patterns during development. Several PcG members contain a protein protein interaction module called a SAM domain (also known as SPM, PNT and HLH). Here we report the high-resolution structure of the SAM domain of polyhomeotic (Ph). Ph-SAM forms a helical polymer structure, providing a likely mechanism for the extension of PcG complexes. The structure of the polymer resembles that formed by the SAM domain of another transcriptional repressor, TEL. The formation of these polymer structures by SAM domains in two divergent repressors suggests a conserved mode of repression involving a higher order chromatin structure. PubMed: 11992127PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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