An investigation of the zinc binding characteristics of the RING finger domain from the human RBBP6 protein using heteronuclear NMR spectroscopy.
Year: 2007
Type: dissertation
Abstract: Retinoblastoma binding protein 6 (RBBP6) is a 250 kDa human splicing-associated protein that is also known to interact with tumour suppressor proteins p53 and pRb and to mediate ubiquitination of p53 via its interaction with Hdm2.RBBP6 is highly up regulated in oesophageal cancer, and has been shown to be a promising target for immunotherapy against the disease.RBBP6 is also known to play a role in mRNA splicing, cell cycle control and apoptosis.RBBP6 contains a RING finger domain, a hallmark of E3 ubiquitin ligases, which is essential for its interaction with Hdm2.RING fingers are well-known structural motifs coordinating two zinc ions in a cross-braced manner by means of eight conserved cysteine or histidine residues.Sequence alignments suggest that the RBBP6 RING finger can be classified as a member of the U box family, which do not require zinc ions in order to fold, although they adopt the same structure as RING fingers, raising the question as to whether zinc is required in order for the RBBP6 RING to fold.
Author: Takalani Mulaudzi
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2230771282