2lq6

Publication Abstract from PubMed

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 beta 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.

Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA.,Liu L, Qin S, Zhang J, Ji P, Shi Y, Wu J J Struct Biol. 2012 Oct;180(1):165-73. doi: 10.1016/j.jsb.2012.06.014. Epub 2012 , Jul 20. PMID:22820306^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.