1urf
From Proteopedia
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| - | [[Image:1urf.gif|left|200px]] | + | [[Image:1urf.gif|left|200px]] |
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| - | '''HR1B DOMAIN FROM PRK1''' | + | {{Structure |
| + | |PDB= 1urf |SIZE=350|CAPTION= <scene name='initialview01'>1urf</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HR1B DOMAIN FROM PRK1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1URF is a [ | + | 1URF 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=1URF OCA]. |
==Reference== | ==Reference== | ||
| - | Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)., Owen D, Lowe PN, Nietlispach D, Brosnan CE, Chirgadze DY, Parker PJ, Blundell TL, Mott HR, J Biol Chem. 2003 Dec 12;278(50):50578-87. Epub 2003 Sep 26. PMID:[http:// | + | Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)., Owen D, Lowe PN, Nietlispach D, Brosnan CE, Chirgadze DY, Parker PJ, Blundell TL, Mott HR, J Biol Chem. 2003 Dec 12;278(50):50578-87. Epub 2003 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14514689 14514689] |
[[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 14:35:42 2008'' |
Revision as of 12:35, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HR1B DOMAIN FROM PRK1
Overview
PRK1 is a serine/threonine kinase that belongs to the protein kinase C superfamily. It can be activated either by members of the Rho family of small G proteins, by proteolysis, or by interaction with lipids. Here we investigate the binding of PRK1 to RhoA and Rac1, two members of the Rho family. We demonstrate that PRK1 binds with a similar affinity to RhoA and Rac1. We present the solution structure of the second HR1 domain from the regulatory N-terminal region of PRK1, and we show that it forms an anti-parallel coiled-coil. In addition, we have used NMR to map the binding contacts of the HR1b domain with Rac1. These are compared with the contacts known to form between HR1a and RhoA. We have used mutagenesis to define the residues in Rac that are important for binding to HR1b. Surprisingly, as well as residues adjacent to Switch I, in Switch II, and in helix alpha5, it appears that the C-terminal stretch of basic amino acids in Rac is required for a high affinity interaction with HR1b.
About this Structure
1URF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)., Owen D, Lowe PN, Nietlispach D, Brosnan CE, Chirgadze DY, Parker PJ, Blundell TL, Mott HR, J Biol Chem. 2003 Dec 12;278(50):50578-87. Epub 2003 Sep 26. PMID:14514689
Page seeded by OCA on Thu Mar 20 14:35:42 2008
Categories: Homo sapiens | Single protein | Blundell, T L. | Brosnan, C E. | Chirgadze, D Y. | Lowe, P N. | Mott, H R. | Nietlispach, D. | Owen, D. | Parker, P J. | Atp-binding | Coiled coil | G-protein | Helical | Hr1 domain | Kinase | Phosphorylation | Serine/threonine-protein kinase | Transferase
