Montoya group publishes in Nature Communications
Today the crystal structure of p15-PAF in complex with PCNA has been published in Nature Communications. Researchers at Novo Nordisk Foundation Center for Protein Research in collaboration with the group of F. Blanco at CIC-Biogune in Bilbao have deciphered the molecular basis of this interaction.
The intrinsically disordered protein p15PAF is overexpressed in cancer and regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. The later is an essential factor in replication and repair that recruits polymerases and other DNA-modifying enzymes to the replication fork. The results of this combined protein-structure function study indicates that p15PAF acts as a flexible drag, which may regulates PCNA sliding along the DNA, thus facilitating the switch from replicative to translesion synthesis polymerases upon DNA damage.The video shows a detailed view of the crystal structure of the p15-PAF/PCNA complex. Each subunit of the PCNA trimer is depicted in surface mode with different colours. The omit map of the p15-PAF molecules is shown in the binding sites where this intrinsically unfolded protein associates.
In this work we have collaborated with a research group consisting of researchers from:
Structural Biology Unit, CIC bioGUNE, Spain
Structural Biology and Biocomputing Programme, Centro Nacional de Investigaciones Oncológicas, Spain
Centre de Biochimie Structurale, INSERM, France
Department of Physical Chemistry and Institute of Biotechnology, Universidad de Granada, Spain
IKERBASQUE, Basque Foundation for Science, Spain
Link to full article at Nature Communications
Authors from Novo Nordisk Foundation Center for Protein Research:
- Gulnahar B. Mortuza
- Guillermo Montoya