3bzi
From Proteopedia
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 3BZI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] Known structural/functional Site: <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Residue+A+1'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BZI OCA]. | + | 3BZI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 2OJS. Active as [http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] Known structural/functional Site: <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Residue+A+1'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BZI OCA]. |
==Reference== | ==Reference== | ||
| Line 30: | Line 30: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:15:40 2008'' |
Revision as of 06:15, 13 February 2008
|
Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization
Overview
Polo-like kinase (Plk1) is crucial for cell cycle progression through, mitosis. Here we present the molecular and structural mechanisms that, regulate the substrate recognition of Plk1 and influence its centrosomal, localization and activity. Our work shows that Plk1 localization is, controlled not only by the polo box domain (PBD); remarkably, the kinase, domain is also involved in Plk1 targeting mechanism to the centrosome. The, crystal structures of the PBD in complex with Cdc25C and Cdc25C-P target, peptides reveal that Trp-414 is fundamental in their recognition, regardless of its phosphorylation status. Binding measurements demonstrate, that W414F mutation abolishes molecular recognition and diminishes, centrosomal localization. Therefore, Plk1 centrosomal localization is not, controlled by His-538 and Lys-540, the residues involved in phosphorylated, target binding. The different conformations of the loop, which connects, the polo boxes in the apo and the PBD-Cdc25C and PBD-Cdc25C-P complex, structures, together with changes in the proline adjacent to the, phosphothreonine in the target peptide, suggest a regulatory mechanism to, detect binding of unphosphorylated or phosphorylated target substrates., Altogether, these data propose a model for the interaction between Plk1, and Cdc25C.
About this Structure
3BZI is a Protein complex structure of sequences from Homo sapiens with as ligand. This structure superseeds the now removed PDB entry 2OJS. Active as Polo kinase, with EC number 2.7.11.21 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization., Garcia-Alvarez B, de Carcer G, Ibanez S, Bragado-Nilsson E, Montoya G, Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3107-12. Epub 2007 Feb 16. PMID:17307877
Page seeded by OCA on Wed Feb 13 08:15:40 2008
