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PDBsum entry 1pls
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Phosphorylation
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PDB id
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1pls
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Contents |
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* Residue conservation analysis
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Nature
369:672-675
(1994)
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PubMed id:
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Solution structure of a pleckstrin-homology domain.
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H.S.Yoon,
P.J.Hajduk,
A.M.Petros,
E.T.Olejniczak,
R.P.Meadows,
S.W.Fesik.
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ABSTRACT
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Pleckstrin, the major protein kinase C substrate of platelets, contains domains
of about 100 amino acids at the amino and carboxy termini that have been found
in a number of proteins, including serine/threonine kinases, GTPase-activating
proteins, phospholipases and cytoskeletal proteins. These conserved sequences,
termed pleckstrin-homology (PH) domains, are thought to be involved in signal
transduction. But the details of the function and binding partners of the PH
domains have not been characterized. Here we report the solution structure of
the N-terminal pleckstrin-homology domain of pleckstrin determined using
heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. The
structure consists of an up-and-down beta-barrel of seven antiparallel
beta-strands and a C-terminal amphiphilic alpha-helix that caps one end of the
barrel. The overall topology of the domain is similar to that of the
retinol-binding protein family of structures.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.A.Clump,
J.J.Yu,
Y.Cho,
R.Gao,
J.Jett,
H.Zot,
J.M.Cunnick,
B.Snyder,
A.C.Clump,
M.Dodrill,
P.Gannett,
J.E.Coad,
R.Shurina,
W.D.Figg,
E.Reed,
and
D.C.Flynn
(2010).
A Polymorphic Variant of AFAP-110 Enhances cSrc Activity.
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Transl Oncol,
3,
276-285.
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Q.Xu,
A.Bateman,
R.D.Finn,
P.Abdubek,
T.Astakhova,
H.L.Axelrod,
C.Bakolitsa,
D.Carlton,
C.Chen,
H.J.Chiu,
M.Chiu,
T.Clayton,
D.Das,
M.C.Deller,
L.Duan,
K.Ellrott,
D.Ernst,
C.L.Farr,
J.Feuerhelm,
J.C.Grant,
A.Grzechnik,
G.W.Han,
L.Jaroszewski,
K.K.Jin,
H.E.Klock,
M.W.Knuth,
P.Kozbial,
S.S.Krishna,
A.Kumar,
D.Marciano,
D.McMullan,
M.D.Miller,
A.T.Morse,
E.Nigoghossian,
A.Nopakun,
L.Okach,
C.Puckett,
R.Reyes,
C.L.Rife,
N.Sefcovic,
H.J.Tien,
C.B.Trame,
H.van den Bedem,
D.Weekes,
T.Wooten,
K.O.Hodgson,
J.Wooley,
M.A.Elsliger,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
and
I.A.Wilson
(2010).
Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain.
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J Mol Biol,
396,
31-46.
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PDB codes:
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Y.H.Huang,
and
K.Sauer
(2010).
Lipid signaling in T-cell development and function.
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Cold Spring Harb Perspect Biol,
2,
a002428.
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J.L.Wilsbacher,
S.L.Moores,
and
J.S.Brugge
(2006).
An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand.
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Cell Commun Signal,
4,
5.
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S.G.Jackson,
Y.Zhang,
X.Bao,
K.Zhang,
R.Summerfield,
R.J.Haslam,
and
M.S.Junop
(2006).
Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 Angstroms.
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Acta Crystallogr D Biol Crystallogr,
62,
324-330.
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PDB code:
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W.Wen,
J.Yan,
and
M.Zhang
(2006).
Structural characterization of the split pleckstrin homology domain in phospholipase C-gamma1 and its interaction with TRPC3.
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J Biol Chem,
281,
12060-12068.
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PDB code:
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C.Edlich,
G.Stier,
B.Simon,
M.Sattler,
and
C.Muhle-Goll
(2005).
Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin.
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Structure,
13,
277-286.
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PDB code:
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J.Yan,
W.Wen,
W.Xu,
J.F.Long,
M.E.Adams,
S.C.Froehner,
and
M.Zhang
(2005).
Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin.
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EMBO J,
24,
3985-3995.
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PDB codes:
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S.Balaji,
M.M.Babu,
L.M.Iyer,
and
L.Aravind
(2005).
Discovery of the principal specific transcription factors of Apicomplexa and their implication for the evolution of the AP2-integrase DNA binding domains.
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Nucleic Acids Res,
33,
3994-4006.
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W.Cho,
and
R.V.Stahelin
(2005).
Membrane-protein interactions in cell signaling and membrane trafficking.
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Annu Rev Biophys Biomol Struct,
34,
119-151.
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G.E.Cozier,
D.Bouyoucef,
and
P.J.Cullen
(2003).
Engineering the phosphoinositide-binding profile of a class I pleckstrin homology domain.
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J Biol Chem,
278,
39489-39496.
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K.S.Yan,
and
M.M.Zhou
(2003).
Examining both sides of a Janus PTB domain.
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Structure,
11,
482-484.
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J.S.Chang,
H.Seok,
T.K.Kwon,
D.S.Min,
B.H.Ahn,
Y.H.Lee,
J.W.Suh,
J.W.Kim,
S.Iwashita,
A.Omori,
S.Ichinose,
O.Numata,
J.K.Seo,
Y.S.Oh,
and
P.G.Suh
(2002).
Interaction of elongation factor-1alpha and pleckstrin homology domain of phospholipase C-gamma 1 with activating its activity.
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J Biol Chem,
277,
19697-19702.
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B.Vanhaesebroeck,
S.J.Leevers,
K.Ahmadi,
J.Timms,
R.Katso,
P.C.Driscoll,
R.Woscholski,
P.J.Parker,
and
M.D.Waterfield
(2001).
Synthesis and function of 3-phosphorylated inositol lipids.
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Annu Rev Biochem,
70,
535-602.
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C.V.Carman,
L.S.Barak,
C.Chen,
L.Y.Liu-Chen,
J.J.Onorato,
S.P.Kennedy,
M.G.Caron,
and
J.L.Benovic
(2000).
Mutational analysis of Gbetagamma and phospholipid interaction with G protein-coupled receptor kinase 2.
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J Biol Chem,
275,
10443-10452.
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J.Beneken,
J.C.Tu,
B.Xiao,
M.Nuriya,
J.P.Yuan,
P.F.Worley,
and
D.J.Leahy
(2000).
Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition.
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Neuron,
26,
143-154.
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PDB codes:
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J.H.Hurley,
and
S.Misra
(2000).
Signaling and subcellular targeting by membrane-binding domains.
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Annu Rev Biophys Biomol Struct,
29,
49-79.
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K.Hamada,
T.Shimizu,
T.Matsui,
S.Tsukita,
and
T.Hakoshima
(2000).
Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.
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EMBO J,
19,
4449-4462.
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PDB codes:
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K.M.Ferguson,
J.M.Kavran,
V.G.Sankaran,
E.Fournier,
S.J.Isakoff,
E.Y.Skolnik,
and
M.A.Lemmon
(2000).
Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains.
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Mol Cell,
6,
373-384.
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PDB codes:
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N.Blomberg,
E.Baraldi,
M.Sattler,
M.Saraste,
and
M.Nilges
(2000).
Structure of a PH domain from the C. elegans muscle protein UNC-89 suggests a novel function.
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Structure,
8,
1079-1087.
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PDB code:
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I.Galetic,
M.Andjelkovic,
R.Meier,
D.Brodbeck,
J.Park,
and
B.A.Hemmings
(1999).
Mechanism of protein kinase B activation by insulin/insulin-like growth factor-1 revealed by specific inhibitors of phosphoinositide 3-kinase--significance for diabetes and cancer.
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Pharmacol Ther,
82,
409-425.
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J.D.Forman-Kay,
and
T.Pawson
(1999).
Diversity in protein recognition by PTB domains.
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Curr Opin Struct Biol,
9,
690-695.
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K.E.Prehoda,
D.J.Lee,
and
W.A.Lim
(1999).
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly.
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Cell,
97,
471-480.
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PDB code:
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L.Yao,
P.Janmey,
L.G.Frigeri,
W.Han,
J.Fujita,
Y.Kawakami,
J.R.Apgar,
and
T.Kawakami
(1999).
Pleckstrin homology domains interact with filamentous actin.
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J Biol Chem,
274,
19752-19761.
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N.Blomberg,
R.R.Gabdoulline,
M.Nilges,
and
R.C.Wade
(1999).
Classification of protein sequences by homology modeling and quantitative analysis of electrostatic similarity.
|
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Proteins,
37,
379-387.
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D.J.Burks,
J.Wang,
H.Towery,
O.Ishibashi,
D.Lowe,
H.Riedel,
and
M.F.White
(1998).
IRS pleckstrin homology domains bind to acidic motifs in proteins.
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J Biol Chem,
273,
31061-31067.
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J.A.Pitcher,
N.J.Freedman,
and
R.J.Lefkowitz
(1998).
G protein-coupled receptor kinases.
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Annu Rev Biochem,
67,
653-692.
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J.M.Kavran,
D.E.Klein,
A.Lee,
M.Falasca,
S.J.Isakoff,
E.Y.Skolnik,
and
M.A.Lemmon
(1998).
Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains.
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J Biol Chem,
273,
30497-30508.
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M.J.Bottomley,
K.Salim,
and
G.Panayotou
(1998).
Phospholipid-binding protein domains.
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Biochim Biophys Acta,
1436,
165-183.
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M.J.Rebecchi,
and
S.Scarlata
(1998).
Pleckstrin homology domains: a common fold with diverse functions.
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Annu Rev Biophys Biomol Struct,
27,
503-528.
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T.F.Martin
(1998).
Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking.
|
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Annu Rev Cell Dev Biol,
14,
231-264.
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X.Liu,
H.Wang,
M.Eberstadt,
A.Schnuchel,
E.T.Olejniczak,
R.P.Meadows,
J.M.Schkeryantz,
D.A.Janowick,
J.E.Harlan,
E.A.Harris,
D.E.Staunton,
and
S.W.Fesik
(1998).
NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
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Cell,
95,
269-277.
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A.D.Ma,
L.F.Brass,
and
C.S.Abrams
(1997).
Pleckstrin associates with plasma membranes and induces the formation of membrane projections: requirements for phosphorylation and the NH2-terminal PH domain.
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J Cell Biol,
136,
1071-1079.
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C.R.Artalejo,
M.A.Lemmon,
J.Schlessinger,
and
H.C.Palfrey
(1997).
Specific role for the PH domain of dynamin-1 in the regulation of rapid endocytosis in adrenal chromaffin cells.
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EMBO J,
16,
1565-1574.
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D.E.Clapham,
and
E.J.Neer
(1997).
G protein beta gamma subunits.
|
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Annu Rev Pharmacol Toxicol,
37,
167-203.
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L.E.Rameh,
A.Arvidsson,
K.L.Carraway,
A.D.Couvillon,
G.Rathbun,
A.Crompton,
B.VanRenterghem,
M.P.Czech,
K.S.Ravichandran,
S.J.Burakoff,
D.S.Wang,
C.S.Chen,
and
L.C.Cantley
(1997).
A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains.
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J Biol Chem,
272,
22059-22066.
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L.Yao,
H.Suzuki,
K.Ozawa,
J.Deng,
C.Lehel,
H.Fukamachi,
W.B.Anderson,
Y.Kawakami,
and
T.Kawakami
(1997).
Interactions between protein kinase C and pleckstrin homology domains. Inhibition by phosphatidylinositol 4,5-bisphosphate and phorbol 12-myristate 13-acetate.
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J Biol Chem,
272,
13033-13039.
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M.Hyvönen,
and
M.Saraste
(1997).
Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia.
|
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EMBO J,
16,
3396-3404.
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PDB code:
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R.M.Cooke
(1997).
Protein NMR extends into new fields of structural biology.
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Curr Opin Chem Biol,
1,
359-364.
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R.M.Scaife,
and
R.L.Margolis
(1997).
The role of the PH domain and SH3 binding domains in dynamin function.
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Cell Signal,
9,
395-401.
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T.T.Chuang,
E.Pompili,
L.Paolucci,
M.Sallese,
L.De Gioia,
M.Salmona,
and
A.De Blasi
(1997).
Identification of a short sequence highly divergent between beta-adrenergic-receptor kinases 1 and 2 that determines the affinity of binding to betagamma subunits of heterotrimeric guanine-nucleotide-binding regulatory proteins.
|
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Eur J Biochem,
245,
533-540.
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W.D.Singer,
H.A.Brown,
and
P.C.Sternweis
(1997).
Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D.
|
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Annu Rev Biochem,
66,
475-509.
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A.Dietrich,
D.Brazil,
O.N.Jensen,
M.Meister,
M.Schrader,
J.F.Moomaw,
M.Mann,
D.Illenberger,
and
P.Gierschik
(1996).
Isoprenylation of the G protein gamma subunit is both necessary and sufficient for beta gamma dimer-mediated stimulation of phospholipase C.
|
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Biochemistry,
35,
15174-15182.
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A.H.Ahn,
C.A.Freener,
E.Gussoni,
M.Yoshida,
E.Ozawa,
and
L.M.Kunkel
(1996).
The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives.
|
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J Biol Chem,
271,
2724-2730.
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A.Viel,
and
D.Branton
(1996).
Spectrin: on the path from structure to function.
|
| |
Curr Opin Cell Biol,
8,
49-55.
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C.S.Abrams,
W.Zhao,
and
L.F.Brass
(1996).
A site of interaction between pleckstrin's PH domains and G beta gamma.
|
| |
Biochim Biophys Acta,
1314,
233-238.
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G.Shaw
(1996).
The pleckstrin homology domain: an intriguing multifunctional protein module.
|
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Bioessays,
18,
35-46.
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H.Konishi,
H.Matsuzaki,
M.Tanaka,
Y.Ono,
C.Tokunaga,
S.Kuroda,
and
U.Kikkawa
(1996).
Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase.
|
| |
Proc Natl Acad Sci U S A,
93,
7639-7643.
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J.A.Pitcher,
Z.L.Fredericks,
W.C.Stone,
R.T.Premont,
R.H.Stoffel,
W.J.Koch,
and
R.J.Lefkowitz
(1996).
Phosphatidylinositol 4,5-bisphosphate (PIP2)-enhanced G protein-coupled receptor kinase (GRK) activity. Location, structure, and regulation of the PIP2 binding site distinguishes the GRK subfamilies.
|
| |
J Biol Chem,
271,
24907-24913.
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J.Font de Mora,
C.Guerrero,
D.Mahadevan,
J.J.Coque,
J.M.Rojas,
L.M.Esteban,
M.Rebecchi,
and
E.Santos
(1996).
Isolated Sos1 PH domain exhibits germinal vesicle breakdown-inducing activity in Xenopus oocytes.
|
| |
J Biol Chem,
271,
18272-18276.
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J.W.Lomasney,
H.F.Cheng,
L.P.Wang,
Y.Kuan,
S.Liu,
S.W.Fesik,
and
K.King
(1996).
Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-delta1 enhances enzyme activity.
|
| |
J Biol Chem,
271,
25316-25326.
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K.Paz,
H.Voliovitch,
Y.R.Hadari,
C.T.Roberts,
D.LeRoith,
and
Y.Zick
(1996).
Interaction between the insulin receptor and its downstream effectors. Use of individually expressed receptor domains for structure/function analysis.
|
| |
J Biol Chem,
271,
6998-7003.
|
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K.Salim,
M.J.Bottomley,
E.Querfurth,
M.J.Zvelebil,
I.Gout,
R.Scaife,
R.L.Margolis,
R.Gigg,
C.I.Smith,
P.C.Driscoll,
M.D.Waterfield,
and
G.Panayotou
(1996).
Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.
|
| |
EMBO J,
15,
6241-6250.
|
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K.Schulz,
S.Danner,
P.Bauer,
S.Schröder,
and
M.J.Lohse
(1996).
Expression of phosducin in a phosducin-negative cell line reveals functions of a Gbetagamma-binding protein.
|
| |
J Biol Chem,
271,
22546-22551.
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|
L.W.Runnels,
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Where a reference describes a PDB structure, the PDB
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