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New page: left|200px<br /> <applet load="2eva" size="450" color="white" frame="true" align="right" spinBox="true" caption="2eva, resolution 2.0Å" /> '''Structural Basis for...
 
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[[Image:2eva.gif|left|200px]]<br />
[[Image:2eva.gif|left|200px]]<br /><applet load="2eva" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2eva" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2eva, resolution 2.0&Aring;" />
caption="2eva, resolution 2.0&Aring;" />
'''Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1'''<br />
'''Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1'''<br />


==Overview==
==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==
==About this Structure==
2EVA 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].  
2EVA 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==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brown, K.]]
[[Category: Brown, K.]]
[[Category: Cheetham, G.M.]]
[[Category: Cheetham, G M.]]
[[Category: Dedi, N.]]
[[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: ADN]]
[[Category: kinase]]
[[Category: kinase]]
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[[Category: tak1]]
[[Category: tak1]]


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