1q4o
From Proteopedia
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The structure of the polo box domain of human Plk1
Overview
Human polo-like kinase Plk1 localizes to the centrosomes, kinetochores and, central spindle structures during mitosis. It plays an essential role in, promoting mitosis and cytokinesis through phosphorylation of a number of, different substrates. Kinase activity is regulated by a conserved, C-terminal domain, termed the polo box domain (PBD), which acts both as an, autoinhibitory domain and as a subcellular localization domain. We have, determined the crystal structure of Plk1 PBD (residues 367-603) to 2.2 A, resolution and the structure of a phospho-peptide-PBD (residues 345-603), complex to 2.3 A resolution. The two polo boxes of the PBD exhibit, identical folds based on a six-stranded beta-sheet and an alpha-helix, despite only 12% sequence identity. The phospho-peptide binds at a site, between the two polo boxes. It makes a short antiparallel beta-sheet, connection and critical contacts to residues Trp414, Leu490, His538 and, Lys540. Most of these residues had been shown to be important for, biological activity through mutational studies. The results provide an, explanation for phospho-peptide recognition and create the basis for new, functional studies.
About this Structure
1Q4O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex., Cheng KY, Lowe ED, Sinclair J, Nigg EA, Johnson LN, EMBO J. 2003 Nov 3;22(21):5757-68. PMID:14592974
Page seeded by OCA on Fri Feb 15 16:42:45 2008
