1gzo: Difference between revisions

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==Overview==

Protein kinase B/Akt plays crucial roles in promoting cell survival and, mediating insulin responses. The enzyme is stimulated by phosphorylation, at two regulatory sites: Thr 309 of the activation segment and Ser 474 of, the hydrophobic motif, a conserved feature of many AGC kinases. Analysis, of the crystal structures of the unphosphorylated and Thr 309, phosphorylated states of the PKB kinase domain provides a molecular, explanation for regulation by Ser 474 phosphorylation. Activation by Ser, 474 phosphorylation occurs via a disorder to order transition of the, alphaC helix with concomitant restructuring of the activation segment and, reconfiguration of the kinase bilobal structure. These conformational, changes are mediated by a phosphorylation-promoted interaction of the, hydrophobic motif with a channel on the N-terminal lobe induced by the, ordered alphaC helix and are mimicked by peptides corresponding to the, hydrophobic motif of PKB and potently by the hydrophobic motif of PRK2.

Protein kinase B/Akt plays crucial roles in promoting cell survival and mediating insulin responses. The enzyme is stimulated by phosphorylation at two regulatory sites: Thr 309 of the activation segment and Ser 474 of the hydrophobic motif, a conserved feature of many AGC kinases. Analysis of the crystal structures of the unphosphorylated and Thr 309 phosphorylated states of the PKB kinase domain provides a molecular explanation for regulation by Ser 474 phosphorylation. Activation by Ser 474 phosphorylation occurs via a disorder to order transition of the alphaC helix with concomitant restructuring of the activation segment and reconfiguration of the kinase bilobal structure. These conformational changes are mediated by a phosphorylation-promoted interaction of the hydrophobic motif with a channel on the N-terminal lobe induced by the ordered alphaC helix and are mimicked by peptides corresponding to the hydrophobic motif of PKB and potently by the hydrophobic motif of PRK2.

==Disease==

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[[Category: Single protein]]

[[Category: Barford, D.]]

[[Category: Hemmings, B.A.]]

[[Category: Hemmings, B A.]]

[[Category: Yang, J.]]

[[Category: atp-binding]]

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[[Category: transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:55:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:47 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Protein kinase B/Akt plays crucial roles in promoting cell survival and, mediating insulin responses. The enzyme is stimulated by phosphorylation, at two regulatory sites: Thr 309 of the activation segment and Ser 474 of, the hydrophobic motif, a conserved feature of many AGC kinases. Analysis, of the crystal structures of the unphosphorylated and Thr 309, phosphorylated states of the PKB kinase domain provides a molecular, explanation for regulation by Ser 474 phosphorylation. Activation by Ser, 474 phosphorylation occurs via a disorder to order transition of the, alphaC helix with concomitant restructuring of the activation segment and, reconfiguration of the kinase bilobal structure. These conformational, changes are mediated by a phosphorylation-promoted interaction of the, hydrophobic motif with a channel on the N-terminal lobe induced by the, ordered alphaC helix and are mimicked by peptides corresponding to the, hydrophobic motif of PKB and potently by the hydrophobic motif of PRK2.
+Protein kinase B/Akt plays crucial roles in promoting cell survival and mediating insulin responses. The enzyme is stimulated by phosphorylation at two regulatory sites: Thr 309 of the activation segment and Ser 474 of the hydrophobic motif, a conserved feature of many AGC kinases. Analysis of the crystal structures of the unphosphorylated and Thr 309 phosphorylated states of the PKB kinase domain provides a molecular explanation for regulation by Ser 474 phosphorylation. Activation by Ser 474 phosphorylation occurs via a disorder to order transition of the alphaC helix with concomitant restructuring of the activation segment and reconfiguration of the kinase bilobal structure. These conformational changes are mediated by a phosphorylation-promoted interaction of the hydrophobic motif with a channel on the N-terminal lobe induced by the ordered alphaC helix and are mimicked by peptides corresponding to the hydrophobic motif of PKB and potently by the hydrophobic motif of PRK2.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Barford, D.]]
-[[Category: Hemmings, B.A.]]
+[[Category: Hemmings, B A.]]
 [[Category: Yang, J.]]
 [[Category: atp-binding]]
@@ Line 23: / Line 23: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:47 2008''