2LQ6

Solution structure of BRD1 PHD2 finger

Summary for 2LQ6

• Entry DOI: 10.2210/pdb2lq6/pdb
• NMR Information: BMRB: 18296
• Descriptor: Bromodomain-containing protein 1, ZINC ION (2 entities in total)
• Functional Keywords: phd finger, metal binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O95696
• Total number of polymer chains: 1
• Total formula weight: 9788.08

Authors

Liu, L.,Wu, J. (deposition date: 2012-02-25, release date: 2012-10-24, Last modification date: 2024-05-01)

Primary citation

Liu, L.,Qin, S.,Zhang, J.,Ji, P.,Shi, Y.,Wu, J.
Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA
J.Struct.Biol., 180:165-173, 2012

PubMed Abstract: Plant homeodomain (PHD) finger is found to be a versatile reader that functions in recruiting transcription factors and chromatin modification complexes. Bromodomain- and PHD finger-containing (BRPF) proteins are identified as scaffold component in a couple of histone acetyltransferase (HATs) complexes but the biological function of PHD fingers, composing the motif called PZPM (PHD/Zn-knuckle/PHD Motif), in BRPF proteins is far from being well understood. Here we report the three-dimensional solution structure of the second PHD finger of PZPM in human BRPF2. According to the structure, BRPF2 PHD2 possesses a two-strand β sheet which is different from any other PHD fingers. Functionally, this PHD finger can potentially bind DNA non-specifically with an evolutionarily conserved and positively charged surface. We provide the structural and interaction information of this atypical PHD finger and categorize this BRPF2 PHD2 into a new subset of PHD finger. Moreover our work also shed light on the functional aspect of the PZPM.

PubMed: 22820306
DOI: 10.1016/j.jsb.2012.06.014

Experimental method

SOLUTION NMR