1w1g
From Proteopedia
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|PDB= 1w1g |SIZE=350|CAPTION= <scene name='initialview01'>1w1g</scene>, resolution 1.45Å | |PDB= 1w1g |SIZE=350|CAPTION= <scene name='initialview01'>1w1g</scene>, resolution 1.45Å | ||
|SITE= <scene name='pdbsite=AC1:4pt+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:4pt+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=4PT:(2R)-3-{[(S)-{[(2S,3R,5S,6S)-2,6-DIHYDROXY-3,4,5-TRIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-(1-HYDROXYBUTOXY)PROPYL BUTYRATE'>4PT</scene> | + | |LIGAND= <scene name='pdbligand=4PT:(2R)-3-{[(S)-{[(2S,3R,5S,6S)-2,6-DIHYDROXY-3,4,5-TRIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-(1-HYDROXYBUTOXY)PROPYL+BUTYRATE'>4PT</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=1w1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w1g OCA], [http://www.ebi.ac.uk/pdbsum/1w1g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w1g RCSB]</span> | ||
}} | }} | ||
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Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates., Komander D, Fairservice A, Deak M, Kular GS, Prescott AR, Peter Downes C, Safrany ST, Alessi DR, van Aalten DM, EMBO J. 2004 Oct 13;23(20):3918-28. Epub 2004 Sep 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15457207 15457207] | Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates., Komander D, Fairservice A, Deak M, Kular GS, Prescott AR, Peter Downes C, Safrany ST, Alessi DR, van Aalten DM, EMBO J. 2004 Oct 13;23(20):3918-28. Epub 2004 Sep 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15457207 15457207] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Transferred entry: 2 7.11 1]] | ||
[[Category: Aalten, D M.F Van.]] | [[Category: Aalten, D M.F Van.]] | ||
[[Category: Alessi, D R.]] | [[Category: Alessi, D R.]] | ||
[[Category: Deak, M.]] | [[Category: Deak, M.]] | ||
[[Category: Komander, D.]] | [[Category: Komander, D.]] | ||
| - | [[Category: 4PT]] | ||
[[Category: inositol phosphate]] | [[Category: inositol phosphate]] | ||
[[Category: pdk1]] | [[Category: pdk1]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''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 00:29:45 2008'' |
Revision as of 21:29, 30 March 2008
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| , resolution 1.45Å | |||||||
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| 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 PDK1 PLECKSTRIN HOMOLOGY (PH) DOMAIN BOUND TO DIC4-PHOSPHATIDYLINOSITOL (3,4,5)-TRISPHOSPHATE
Overview
3-phosphoinositide-dependent protein kinase-1 (PDK1) phosphorylates and activates many kinases belonging to the AGC subfamily. PDK1 possesses a C-terminal pleckstrin homology (PH) domain that interacts with PtdIns(3,4,5)P3/PtdIns(3,4)P2 and with lower affinity to PtdIns(4,5)P2. We describe the crystal structure of the PDK1 PH domain, in the absence and presence of PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4. The structures reveal a 'budded' PH domain fold, possessing an N-terminal extension forming an integral part of the overall fold, and display an unusually spacious ligand-binding site. Mutagenesis and lipid-binding studies were used to define the contribution of residues involved in phosphoinositide binding. Using a novel quantitative binding assay, we found that Ins(1,3,4,5,6)P5 and InsP6, which are present at micromolar levels in the cytosol, interact with full-length PDK1 with nanomolar affinities. Utilising the isolated PDK1 PH domain, which has reduced affinity for Ins(1,3,4,5,6)P5/InsP6, we perform localisation studies that suggest that these inositol phosphates serve to anchor a portion of cellular PDK1 in the cytosol, where it could activate its substrates such as p70 S6-kinase and p90 ribosomal S6 kinase that do not interact with phosphoinositides.
About this Structure
1W1G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates., Komander D, Fairservice A, Deak M, Kular GS, Prescott AR, Peter Downes C, Safrany ST, Alessi DR, van Aalten DM, EMBO J. 2004 Oct 13;23(20):3918-28. Epub 2004 Sep 30. PMID:15457207
Page seeded by OCA on Mon Mar 31 00:29:45 2008
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Single protein | Aalten, D M.F Van. | Alessi, D R. | Deak, M. | Komander, D. | Inositol phosphate | Pdk1 | Phosphoinositide | Phosphoinositide dependent protein kinase 1 | Pi3-kinase | Pip3 serine/threonine protein kinase | Pkb | Pleckstrin homology domain | Signal transduction
