2bdw: Difference between revisions

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==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.

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==

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[[Category: Single protein]]

[[Category: Kuriyan, J.]]

[[Category: Rosenberg, O.S.]]

[[Category: Rosenberg, O S.]]

[[Category: kinase; calmodulin activated]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jan 29 18~~:22:22 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:44 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Kuriyan, J.]]
-[[Category: Rosenberg, O.S.]]
+[[Category: Rosenberg, O S.]]
 [[Category: kinase; calmodulin activated]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:22:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:44 2008''