3L42

PWWP domain of human bromodomain and PHD finger containing protein 1

Summary for 3L42

• Entry DOI: 10.2210/pdb3l42/pdb
• Descriptor: Peregrin, UNKNOWN ATOM OR ION (3 entities in total)
• Functional Keywords: transcription regulation, histone h3 acetylation, chromatin modification, structural genomics, structural genomics consortium, sgc, activator, bromodomain, chromatin regulator, dna-binding, metal-binding, nucleus, phosphoprotein, transcription, zinc-finger
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : P55201
• Total number of polymer chains: 1
• Total formula weight: 15076.45

Authors

Tempel, W.,Zeng, H.,Ni, S.,Amaya, M.F.,Dong, A.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Wu, H.,Structural Genomics Consortium (SGC) (deposition date: 2009-12-18, release date: 2010-01-12, Last modification date: 2024-02-21)

Primary citation

Wu, H.,Zeng, H.,Lam, R.,Tempel, W.,Amaya, M.F.,Xu, C.,Dombrovski, L.,Qiu, W.,Wang, Y.,Min, J.
Structural and Histone Binding Ability Characterizations of Human PWWP Domains.
Plos One, 6:e18919-e18919, 2011

PubMed Abstract: The PWWP domain was first identified as a structural motif of 100-130 amino acids in the WHSC1 protein and predicted to be a protein-protein interaction domain. It belongs to the Tudor domain 'Royal Family', which consists of Tudor, chromodomain, MBT and PWWP domains. While Tudor, chromodomain and MBT domains have long been known to bind methylated histones, PWWP was shown to exhibit histone binding ability only until recently.

PubMed: 21720545
DOI: 10.1371/journal.pone.0018919

Experimental method

X-RAY DIFFRACTION (1.3 Å)