Ontology highlight
ABSTRACT:
SUBMITTER: Yun SM
PROVIDER: S-EPMC2721907 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Yun Sang-Moon SM Moulaei Tinoush T Lim Dan D Bang Jeong K JK Park Jung-Eun JE Shenoy Shilpa R SR Liu Fa F Kang Young H YH Liao Chenzhong C Soung Nak-Kyun NK Lee Sunhee S Yoon Do-Young DY Lim Yoongho Y Lee Dong-Hee DH Otaka Akira A Appella Ettore E McMahon James B JB Nicklaus Marc C MC Burke Terrence R TR Yaffe Michael B MB Wlodawer Alexander A Lee Kyung S KS
Nature structural & molecular biology 20090713 8
Polo-like kinase-1 (Plk1) has a pivotal role in cell proliferation and is considered a potential target for anticancer therapy. The noncatalytic polo-box domain (PBD) of Plk1 forms a phosphoepitope binding module for protein-protein interaction. Here, we report the identification of minimal phosphopeptides that specifically interact with the PBD of human PLK1, but not those of the closely related PLK2 and PLK3. Comparative binding studies and analyses of crystal structures of the PLK1 PBD in com ...[more]