1w1h: Difference between revisions

Revision as of 19:50, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1w1h.png

1w1h, resolution 1.45Å ()

Ligands:

,

Activity:

Non-specific serine/threonine protein kinase, with EC number 2.7.11.1

Related:

1h1w, 1oky, 1okz, 1uu3, 1uu7, 1uu8, 1uu9, 1uvr, 1w1d, 1w1g

Structural annotation:
Resources:	CATH : 1W1Ha00, 1W1Hb00, 1W1Hc00, 1W1Hd00 InterPro : Ipr011993, Ipr015746, Ipr011009, Ipr002290, Ipr000719, Ipr001849, Ipr008271 UniProt : O15530

Functional annotation:
Cellular component:	membrane plasma membrane cytoplasm
Biological process:	insulin receptor signaling pathway intracellular signaling cascade protein amino acid phosphorylation actin cytoskeleton organization and biogenesis
Molecular function:	protein serine/threonine kinase activity protein kinase activity protein binding ATP binding kinase activity transferase activity nucleotide binding 3-phosphoinositide-dependent protein kinase activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN HOMOLOGY (PH) DOMAINCRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN HOMOLOGY (PH) DOMAIN

Template:ABSTRACT PUBMED 15457207

About this StructureAbout this Structure

1W1H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Jul 28 19:50:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1w1h|  PDB=1w1h  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN HOMOLOGY (PH) DOMAIN'''
+===CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN HOMOLOGY (PH) DOMAIN===
-==Overview==
+<!--
--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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15457207}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15457207 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15457207}}
 ==About this Structure==
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 [[Category: Signal transduction]]
 [[Category: Transferase]]
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