1w3b: Difference between revisions

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==Overview==

Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of, intracellular glycosylation catalyzed by the conserved O-linked GlcNAc, transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide, (TPR) repeats that mediates the recognition of a broad range of target, proteins. Components of the nuclear pore complex are major OGT targets, as, OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc, modification at the nuclear envelope. To gain insight into the mechanism, of target recognition, we solved the crystal structure of the homodimeric, TPR domain of human OGT, which contains 11.5 TPR repeats. The repeats form, an elongated superhelix. The concave surface of the superhelix is lined by, absolutely conserved asparagines, in a manner reminiscent of the, peptide-binding site of importin alpha. Based on this structural, similarity, we propose that OGT uses an analogous molecular mechanism to, recognize its targets.

Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of intracellular glycosylation catalyzed by the conserved O-linked GlcNAc transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide (TPR) repeats that mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope. To gain insight into the mechanism of target recognition, we solved the crystal structure of the homodimeric TPR domain of human OGT, which contains 11.5 TPR repeats. The repeats form an elongated superhelix. The concave surface of the superhelix is lined by absolutely conserved asparagines, in a manner reminiscent of the peptide-binding site of importin alpha. Based on this structural similarity, we propose that OGT uses an analogous molecular mechanism to recognize its targets.

==About this Structure==

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[[Category: Single protein]]

[[Category: Conti, E.]]

[[Category: Hanover, J.A.]]

[[Category: Hanover, J A.]]

[[Category: Izaurralde, E.]]

[[Category: Jinek, M.]]

[[Category: Lazarus, B.D.]]

[[Category: Lazarus, B D.]]

[[Category: Rehwinkel, J.]]

[[Category: CA]]

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[[Category: transferase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:59 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of, intracellular glycosylation catalyzed by the conserved O-linked GlcNAc, transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide, (TPR) repeats that mediates the recognition of a broad range of target, proteins. Components of the nuclear pore complex are major OGT targets, as, OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc, modification at the nuclear envelope. To gain insight into the mechanism, of target recognition, we solved the crystal structure of the homodimeric, TPR domain of human OGT, which contains 11.5 TPR repeats. The repeats form, an elongated superhelix. The concave surface of the superhelix is lined by, absolutely conserved asparagines, in a manner reminiscent of the, peptide-binding site of importin alpha. Based on this structural, similarity, we propose that OGT uses an analogous molecular mechanism to, recognize its targets.
+Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of intracellular glycosylation catalyzed by the conserved O-linked GlcNAc transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide (TPR) repeats that mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope. To gain insight into the mechanism of target recognition, we solved the crystal structure of the homodimeric TPR domain of human OGT, which contains 11.5 TPR repeats. The repeats form an elongated superhelix. The concave surface of the superhelix is lined by absolutely conserved asparagines, in a manner reminiscent of the peptide-binding site of importin alpha. Based on this structural similarity, we propose that OGT uses an analogous molecular mechanism to recognize its targets.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Conti, E.]]
-[[Category: Hanover, J.A.]]
+[[Category: Hanover, J A.]]
 [[Category: Izaurralde, E.]]
 [[Category: Jinek, M.]]
-[[Category: Lazarus, B.D.]]
+[[Category: Lazarus, B D.]]
 [[Category: Rehwinkel, J.]]
 [[Category: CA]]
@@ Line 29: / Line 29: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:18:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:59 2008''