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| {{STRUCTURE_1umw| PDB=1umw | SCENE= }} | | {{STRUCTURE_1umw| PDB=1umw | SCENE= }} |
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| '''STRUCTURE OF A HUMAN PLK1 POLO-BOX DOMAIN/PHOSPHOPEPTIDE COMPLEX'''
| | ===STRUCTURE OF A HUMAN PLK1 POLO-BOX DOMAIN/PHOSPHOPEPTIDE COMPLEX=== |
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| ==Overview==
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| Polo-like kinases (Plks) perform crucial functions in cell-cycle progression and multiple stages of mitosis. Plks are characterized by a C-terminal noncatalytic region containing two tandem Polo boxes, termed the Polo-box domain (PBD), which has recently been implicated in phosphodependent substrate targeting. We show that the PBDs of human, Xenopus, and yeast Plks all recognize similar phosphoserine/threonine-containing motifs. The 1.9 A X-ray structure of a human Plk1 PBD-phosphopeptide complex shows that the Polo boxes each comprise beta6alpha structures that associate to form a 12-stranded beta sandwich domain. The phosphopeptide binds along a conserved, positively charged cleft located at the edge of the Polo-box interface. Mutations that specifically disrupt phosphodependent interactions abolish cell-cycle-dependent localization and provide compelling phenotypic evidence that PBD-phospholigand binding is necessary for proper mitotic progression. In addition, phosphopeptide binding to the PBD stimulates kinase activity in full-length Plk1, suggesting a conformational switching mechanism for Plk regulation and a dual functionality for the PBD.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14532005}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14532005 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14532005}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Phosphopeptide-binding domain]] | | [[Category: Phosphopeptide-binding domain]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:26:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:27:40 2008'' |
