2eva: Difference between revisions

Revision as of 18:15, 21 February 2008

Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1

OverviewOverview

Transforming growth factor-beta (TGF-beta)-activated kinase 1 (TAK1) is a member of the MAPKKK family of protein kinases, and is involved in intracellular signalling pathways stimulated by transforming growth factor beta, interleukin-1 and tumour necrosis factor-alpha. TAK1 is known to rely upon an additional protein, TAK1-binding protein 1 (TAB1), for complete activation. However, the molecular basis for this activation has yet to be elucidated. We have solved the crystal structure of a novel TAK1 chimeric protein and these data give insight into how TAK1 is activated by TAB1. Our results reveal a novel binding pocket on the TAK1 kinase domain whose shape complements that of a unique alpha-helix in the TAK1 binding domain of TAB1, providing the basis for an intimate hydrophobic association between the protein activator and its target.

About this StructureAbout this Structure

2EVA is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the interaction of TAK1 kinase with its activating protein TAB1., Brown K, Vial SC, Dedi N, Long JM, Dunster NJ, Cheetham GM, J Mol Biol. 2005 Dec 16;354(5):1013-20. Epub 2005 Nov 2. PMID:16289117

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OCA

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 '''Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1'''<br />
 ==Overview==
-Transforming growth factor-beta (TGF-beta)-activated kinase 1 (TAK1) is a, member of the MAPKKK family of protein kinases, and is involved in, intracellular signalling pathways stimulated by transforming growth factor, beta, interleukin-1 and tumour necrosis factor-alpha. TAK1 is known to, rely upon an additional protein, TAK1-binding protein 1 (TAB1), for, complete activation. However, the molecular basis for this activation has, yet to be elucidated. We have solved the crystal structure of a novel TAK1, chimeric protein and these data give insight into how TAK1 is activated by, TAB1. Our results reveal a novel binding pocket on the TAK1 kinase domain, whose shape complements that of a unique alpha-helix in the TAK1 binding, domain of TAB1, providing the basis for an intimate hydrophobic, association between the protein activator and its target.
+Transforming growth factor-beta (TGF-beta)-activated kinase 1 (TAK1) is a member of the MAPKKK family of protein kinases, and is involved in intracellular signalling pathways stimulated by transforming growth factor beta, interleukin-1 and tumour necrosis factor-alpha. TAK1 is known to rely upon an additional protein, TAK1-binding protein 1 (TAB1), for complete activation. However, the molecular basis for this activation has yet to be elucidated. We have solved the crystal structure of a novel TAK1 chimeric protein and these data give insight into how TAK1 is activated by TAB1. Our results reveal a novel binding pocket on the TAK1 kinase domain whose shape complements that of a unique alpha-helix in the TAK1 binding domain of TAB1, providing the basis for an intimate hydrophobic association between the protein activator and its target.
 ==About this Structure==
-EVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ADN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EVA OCA].
+EVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ADN:'>ADN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVA OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Brown, K.]]
-[[Category: Cheetham, G.M.]]
+[[Category: Cheetham, G M.]]
 [[Category: Dedi, N.]]
-[[Category: Dunster, N.J.]]
+[[Category: Dunster, N J.]]
-[[Category: Long, J.M.]]
+[[Category: Long, J M.]]
-[[Category: Vial, S.C.]]
+[[Category: Vial, S C.]]
 [[Category: ADN]]
 [[Category: kinase]]
@@ Line 26: / Line 25: @@
 [[Category: tak1]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:56:12 2007''
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