2c30: Difference between revisions
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==Overview== | ==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, .. | 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, residues that structurally link the glycine-rich loop, alphaC, and the, activation segment and firmly anchor alphaC in an active conformation., Inhibitor screening identified six potent PAK inhibitors from which a, tri-substituted purine inhibitor was cocrystallized with PAK4 and PAK5. | ||
==About this Structure== | ==About this Structure== | ||
2C30 is a | 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: transferase]] | [[Category: transferase]] | ||
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Revision as of 14:42, 5 November 2007
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CRYSTAL STRUCTURE OF THE HUMAN P21-ACTIVATED KINASE 6
OverviewOverview
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, residues that structurally link the glycine-rich loop, alphaC, and the, activation segment and firmly anchor alphaC in an active conformation., Inhibitor screening identified six potent PAK inhibitors from which a, tri-substituted purine inhibitor was cocrystallized with PAK4 and PAK5.
About this StructureAbout 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.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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