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1umw

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[[Image:1umw.gif|left|200px]]
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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'''
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===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.
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{{ABSTRACT_PUBMED_14532005}}
==About this Structure==
==About this Structure==
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[[Category: Phosphopeptide-binding domain]]
[[Category: Phosphopeptide-binding domain]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:26:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:27:40 2008''

Revision as of 04:27, 28 July 2008

Template:STRUCTURE 1umw

STRUCTURE OF A HUMAN PLK1 POLO-BOX DOMAIN/PHOSPHOPEPTIDE COMPLEX

Template:ABSTRACT PUBMED 14532005

About this Structure

1UMW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain., Elia AE, Rellos P, Haire LF, Chao JW, Ivins FJ, Hoepker K, Mohammad D, Cantley LC, Smerdon SJ, Yaffe MB, Cell. 2003 Oct 3;115(1):83-95. PMID:14532005

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