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4YJ0

Crystal structure of the DM domain of human DMRT1 bound to 25mer target DNA

Summary for 4YJ0
Entry DOI10.2210/pdb4yj0/pdb
DescriptorDoublesex- and mab-3-related transcription factor 1, DNA (25-MER), ZINC ION, ... (4 entities in total)
Functional Keywordstranscription factor, protein-dna complex, double zn-finger, transcription
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains5
Total formula weight40208.27
Authors
Murphy, M.W.,Lee, J.K.,Rojo, S.,Gearhart, M.D.,Kurahashi, K.,Banerjee, S.,Loeuille, G.,Bashamboo, A.,McElreavey, K.,Zarkower, D.,Aihara, H.,Bardwell, V.J. (deposition date: 2015-03-02, release date: 2015-05-27, Last modification date: 2024-06-19)
Primary citationMurphy, M.W.,Lee, J.K.,Rojo, S.,Gearhart, M.D.,Kurahashi, K.,Banerjee, S.,Loeuille, G.A.,Bashamboo, A.,McElreavey, K.,Zarkower, D.,Aihara, H.,Bardwell, V.J.
An ancient protein-DNA interaction underlying metazoan sex determination.
Nat.Struct.Mol.Biol., 22:442-451, 2015
Cited by
PubMed Abstract: DMRT transcription factors are deeply conserved regulators of metazoan sexual development. They share the DM DNA-binding domain, a unique intertwined double zinc-binding module followed by a C-terminal recognition helix, which binds a pseudopalindromic target DNA. Here we show that DMRT proteins use a unique binding interaction, inserting two adjacent antiparallel recognition helices into a widened DNA major groove to make base-specific contacts. Versatility in how specific base contacts are made allows human DMRT1 to use multiple DNA binding modes (tetramer, trimer and dimer). Chromatin immunoprecipitation with exonuclease treatment (ChIP-exo) indicates that multiple DNA binding modes also are used in vivo. We show that mutations affecting residues crucial for DNA recognition are associated with an intersex phenotype in flies and with male-to-female sex reversal in humans. Our results illuminate an ancient molecular interaction underlying much of metazoan sexual development.
PubMed: 26005864
DOI: 10.1038/nsmb.3032
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.814 Å)
Structure validation

243083

数据于2025-10-15公开中

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