2C7H

Solution NMR structure of the DWNN domain from human RBBP6

Summary for 2C7H

Entry DOI	10.2210/pdb2c7h/pdb
Descriptor	RETINOBLASTOMA-BINDING PROTEIN 6, ISOFORM 3 (1 entity in total)
Functional Keywords	rbbp6, p53-associated, mrna processing, splicing-associated, oesophageal cancer, ubiquitin-like protein
Biological source	HOMO SAPIENS (HUMAN)
Total number of polymer chains	1
Total formula weight	9544.00
Authors	Pugh, D.J.R.,Ab, E.,Faro, A.,Lutya, P.T.,Hoffmann, E.,Rees, D.J.G. (deposition date: 2005-11-24, release date: 2006-01-19, Last modification date: 2024-05-15)
Primary citation	Pugh, D.J.R.,Ab, E.,Faro, A.,Lutya, P.T.,Hoffmann, E.,Rees, D.J.G. Dwnn, a Novel Ubiquitin-Like Domain, Implicates Rbbp6 in Mrna Processing and Ubiquitin-Like Pathways Bmc Struct.Biol., 6:1-, 2006 Cited by PubMed Abstract: RBBP6 is a 250 kDa splicing-associated protein that has been identified as an E3 ligase due to the presence of a RING finger domain. In humans and mice it interacts with both p53 and Rb, and plays a role in the induction of apoptosis and regulation of the cell cycle. RBBP6 has recently been shown to be highly up-regulated in oesophageal cancer, and to be a promising target for immunotherapy against the disease. PubMed: 16396680 DOI: 10.1186/1472-6807-6-1 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation