1q4o
From Proteopedia
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| - | [[Image:1q4o.jpg|left|200px]] | + | [[Image:1q4o.jpg|left|200px]] |
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| - | '''The structure of the polo box domain of human Plk1''' | + | {{Structure |
| + | |PDB= 1q4o |SIZE=350|CAPTION= <scene name='initialview01'>1q4o</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= PLK OR PLK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''The structure of the polo box domain of human Plk1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q4O is a [ | + | 1Q4O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4O OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14592974 14592974] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:32:56 2008'' |
Revision as of 11:32, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PLK OR PLK1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:32:56 2008
