2c30: Difference between revisions
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|PDB= 2c30 |SIZE=350|CAPTION= <scene name='initialview01'>2c30</scene>, resolution 1.60Å | |PDB= 2c30 |SIZE=350|CAPTION= <scene name='initialview01'>2c30</scene>, resolution 1.60Å | ||
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/ | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c30 OCA], [http://www.ebi.ac.uk/pdbsum/2c30 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c30 RCSB]</span> | |||
}} | }} | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17292838 17292838] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17292838 17292838] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arrowsmith, C.]] | [[Category: Arrowsmith, C.]] | ||
[[Category: Berridge, G.]] | [[Category: Berridge, G.]] | ||
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[[Category: Turnbull, A.]] | [[Category: Turnbull, A.]] | ||
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
[[Category: crib domain]] | [[Category: crib domain]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:32 2008'' | ||
Revision as of 02:15, 31 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 02:15:32 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Non-specific serine/threonine protein kinase
- Single protein
- 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.
- Atp-binding
- Crib domain
- Kinase
- Nucleotide-binding
- Phosphorylation
- Polymorphism
- Serine-threonine protein kinase
- Ste20-like
- Transferase