2c30
From Proteopedia
(New page: 200px<br /> <applet load="2c30" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c30, resolution 1.60Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2C30 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 PO4 and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C30 OCA]]. | + | 2C30 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 PO4 and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C30 OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Transferred entry: 2.7.11.1]] | ||
[[Category: Arrowsmith, C.]] | [[Category: Arrowsmith, C.]] | ||
[[Category: Berridge, G.]] | [[Category: Berridge, G.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:11:17 2007'' |
Revision as of 10:06, 30 October 2007
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CRYSTAL STRUCTURE OF THE HUMAN P21-ACTIVATED KINASE 6
Overview
p21-activated kinases have been classified into two groups based on their, domain architecture. Group II PAKs (PAK4-6) regulate a wide variety of, cellular functions, and PAK deregulation has been linked to tumor, development. Structural comparison of five high-resolution structures, comprising all active, monophosphorylated group II catalytic domains, revealed a surprising degree of domain plasticity, including a number of, catalytically productive and nonproductive conformers. Rearrangements of, helix alphaC, a key regulatory element of kinase function, resulted in an, additional helical turn at the alphaC N terminus and a distortion of its C, terminus, a movement hitherto unseen in protein kinases. The observed, structural changes led to the formation of interactions between conserved, ... [(full description)]
About this Structure
2C30 is a [Single protein] structure of sequence from [Homo sapiens] with PO4 and CL as [ligands]. Active as [Transferred entry: 2.7.11.1], with EC number [2.7.1.37]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs., Eswaran J, Lee WH, Debreczeni JE, Filippakopoulos P, Turnbull A, Fedorov O, Deacon SW, Peterson JR, Knapp S, Structure. 2007 Feb;15(2):201-13. PMID:17292838
Page seeded by OCA on Tue Oct 30 12:11:17 2007
Categories: Homo sapiens | Single protein | Transferred entry: 2.7.11.1 | Arrowsmith, C. | Berridge, G. | Bray, J. | Burgess, N. | Colebrook, S. | Das, S. | Delft, F.Von. | Edwards, A. | Eswaran, J. | Filippakopoulos, P. | Gileadi, O. | Knapp, S. | Papagrigoriou, E. | Savitsky, P. | Smee, C. | Sundstrom, M. | Turnbull, A. | Weigelt, J. | CL | PO4 | Atp-binding | Crib domain | Kinase | Nucleotide-binding | Phosphorylation | Polymorphism | Serine-threonine protein kinase | Ste20-like | Transferase
