2iwr: Difference between revisions

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==Overview==

Centaurins are a family of proteins that contain GTPase-activating protein, domains, with the gamma family members containing in addition a, GTPase-like domain. Centaurins reside mainly in the nucleus and are known, to activate phosphoinositide 3-kinase, a key regulator of cell, proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding, studies, we show that, for CENTG1 (centaurin gamma-1) the GTPase-like, domain has broader trinucleotide specificity. Alterations within the G4, motif of CENTG1 from the highly conserved NKXD found in typical GTPases to, TQDR result in the loss of specificity, a lower affinity for the, nucleotides and higher turnover rates. These results indicate that the, centaurins could be more accurately classified as NTPases and point to, alternative mechanisms of cell signalling control.

Centaurins are a family of proteins that contain GTPase-activating protein domains, with the gamma family members containing in addition a GTPase-like domain. Centaurins reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding studies, we show that, for CENTG1 (centaurin gamma-1) the GTPase-like domain has broader trinucleotide specificity. Alterations within the G4 motif of CENTG1 from the highly conserved NKXD found in typical GTPases to TQDR result in the loss of specificity, a lower affinity for the nucleotides and higher turnover rates. These results indicate that the centaurins could be more accurately classified as NTPases and point to alternative mechanisms of cell signalling control.

==About this Structure==

Line 14:

[[Category: Single protein]]

[[Category: Arrowsmith, C.]]

[[Category: Doyle, D.A.]]

[[Category: Doyle, D A.]]

[[Category: Edwards, A.]]

[[Category: Elkins, J.M.]]

[[Category: Elkins, J M.]]

[[Category: Papagrigoriou, E.]]

[[Category: Sgc, Structural.Genomics.Consortium.]]

[[Category: Sgc, Structural Genomics Consortium.]]

[[Category: Soundararajan, M.]]

[[Category: Sundstrom, M.]]

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[[Category: zinc-finger]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 12~~:19:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:47 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Centaurins are a family of proteins that contain GTPase-activating protein, domains, with the gamma family members containing in addition a, GTPase-like domain. Centaurins reside mainly in the nucleus and are known, to activate phosphoinositide 3-kinase, a key regulator of cell, proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding, studies, we show that, for CENTG1 (centaurin gamma-1) the GTPase-like, domain has broader trinucleotide specificity. Alterations within the G4, motif of CENTG1 from the highly conserved NKXD found in typical GTPases to, TQDR result in the loss of specificity, a lower affinity for the, nucleotides and higher turnover rates. These results indicate that the, centaurins could be more accurately classified as NTPases and point to, alternative mechanisms of cell signalling control.
+Centaurins are a family of proteins that contain GTPase-activating protein domains, with the gamma family members containing in addition a GTPase-like domain. Centaurins reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding studies, we show that, for CENTG1 (centaurin gamma-1) the GTPase-like domain has broader trinucleotide specificity. Alterations within the G4 motif of CENTG1 from the highly conserved NKXD found in typical GTPases to TQDR result in the loss of specificity, a lower affinity for the nucleotides and higher turnover rates. These results indicate that the centaurins could be more accurately classified as NTPases and point to alternative mechanisms of cell signalling control.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Arrowsmith, C.]]
-[[Category: Doyle, D.A.]]
+[[Category: Doyle, D A.]]
 [[Category: Edwards, A.]]
-[[Category: Elkins, J.M.]]
+[[Category: Elkins, J M.]]
 [[Category: Papagrigoriou, E.]]
-[[Category: Sgc, Structural.Genomics.Consortium.]]
+[[Category: Sgc, Structural Genomics Consortium.]]
 [[Category: Soundararajan, M.]]
 [[Category: Sundstrom, M.]]
@@ Line 45: / Line 45: @@
 [[Category: zinc-finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:19:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:47 2008''