2bdw
From Proteopedia
(New page: 200px<br /><applet load="2bdw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bdw, resolution 1.80Å" /> '''Crystal Structure of...) |
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==Overview== | ==Overview== | ||
| - | Ca2+/calmodulin-dependent protein kinase-II (CaMKII) is unique among | + | Ca2+/calmodulin-dependent protein kinase-II (CaMKII) is unique among protein kinases for its dodecameric assembly and its complex response to Ca2+. The crystal structure of the autoinhibited kinase domain of CaMKII, determined at 1.8 A resolution, reveals an unexpected dimeric organization in which the calmodulin-responsive regulatory segments form a coiled-coil strut that blocks peptide and ATP binding to the otherwise intrinsically active kinase domains. A threonine residue in the regulatory segment, which when phosphorylated renders CaMKII calmodulin independent, is held apart from the catalytic sites by the organization of the dimer. This ensures a strict Ca2+ dependence for initial activation. The structure of the kinase dimer, when combined with small-angle X-ray scattering data for the holoenzyme, suggests that inactive CaMKII forms tightly packed autoinhibited assemblies that convert upon activation into clusters of loosely tethered and independent kinase domains. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
| - | [[Category: Rosenberg, O | + | [[Category: Rosenberg, O S.]] |
[[Category: kinase; calmodulin activated]] | [[Category: kinase; calmodulin activated]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:44 2008'' |
Revision as of 14:36, 21 February 2008
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Crystal Structure of the Auto-Inhibited Kinase Domain of Calcium/Calmodulin Activated Kinase II
Overview
Ca2+/calmodulin-dependent protein kinase-II (CaMKII) is unique among protein kinases for its dodecameric assembly and its complex response to Ca2+. The crystal structure of the autoinhibited kinase domain of CaMKII, determined at 1.8 A resolution, reveals an unexpected dimeric organization in which the calmodulin-responsive regulatory segments form a coiled-coil strut that blocks peptide and ATP binding to the otherwise intrinsically active kinase domains. A threonine residue in the regulatory segment, which when phosphorylated renders CaMKII calmodulin independent, is held apart from the catalytic sites by the organization of the dimer. This ensures a strict Ca2+ dependence for initial activation. The structure of the kinase dimer, when combined with small-angle X-ray scattering data for the holoenzyme, suggests that inactive CaMKII forms tightly packed autoinhibited assemblies that convert upon activation into clusters of loosely tethered and independent kinase domains.
About this Structure
2BDW is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme., Rosenberg OS, Deindl S, Sung RJ, Nairn AC, Kuriyan J, Cell. 2005 Dec 2;123(5):849-60. PMID:16325579
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