PDBsum entry 1pms

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Signal transduction PDB id
Protein chain
135 a.a. *
* Residue conservation analysis
PDB id:
Name: Signal transduction
Title: Pleckstrin homology domain of son of sevenless 1 (sos1) with glycine-serine added to the n-terminus, nmr, 20 structures
Structure: Sos 1. Chain: a. Fragment: pleckstrin homology domain. Synonym: son of sevenless. Engineered: yes. Mutation: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: S.Koshiba,T.Kigawa,J.Kim,M.Shirouzu,D.Bowtell,S.Yokoyama, Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref:
S.Koshiba et al. (1997). The solution structure of the pleckstrin homology domain of mouse Son-of-sevenless 1 (mSos1). J Mol Biol, 269, 579-591. PubMed id: 9217262 DOI: 10.1006/jmbi.1997.1041
18-Feb-97     Release date:   15-May-97    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q62245  (SOS1_MOUSE) -  Son of sevenless homolog 1
1319 a.a.
135 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   1 term 
  Biological process     small GTPase mediated signal transduction   1 term 
  Biochemical function     guanyl-nucleotide exchange factor activity     1 term  


DOI no: 10.1006/jmbi.1997.1041 J Mol Biol 269:579-591 (1997)
PubMed id: 9217262  
The solution structure of the pleckstrin homology domain of mouse Son-of-sevenless 1 (mSos1).
S.Koshiba, T.Kigawa, J.H.Kim, M.Shirouzu, D.Bowtell, S.Yokoyama.
The solution structure of the pleckstrin homology (PH) domain of mouse Son-of-sevenless 1 (mSos1), a guanine nucleotide exchange factor for Ras, was determined by multidimensional NMR spectroscopy. The structure of the mSos1 PH domain involves the fundamental PH fold, consisting of seven beta-strands and one alpha-helix at the C terminus, as determined for the PH domains of other proteins. By contrast, the mSos1 PH domain showed two major characteristic features. First, the N-terminal region, whose amino acid sequence is highly conserved among Sos proteins, was found to form an alpha-helix, which interacts with the beta-sheet structure of the fundamental PH fold. Second, there is a long unstructured loop between beta3 and beta4. Furthermore, the mSos1 PH domain was found to bind phosphatidylinositol-4,5-bisphosphate by a centrifugation assay. The addition of inositol-1,4,5-trisphosphate to the mSos1 PH domain induced backbone amide chemical shift changes mainly in the beta1/beta2 loop and the N- and C-terminal parts of the long beta3/beta4 loop. This inositol-1,4,5-trisphosphate-binding mode of the mSos1 PH domain is somewhat similar to those of the PH domains of pleckstrin and phospholipase Cdelta1, and is clearly different from those of other PH domains.
  Selected figure(s)  
Figure 4.
Figure 7.
Figure 7. Schematic representation of the interface between the N-terminal α-helix and the first β-sheet. NOE connectivities are indicated with arrows.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1997, 269, 579-591) copyright 1997.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20133692 J.Gureasko, O.Kuchment, D.L.Makino, H.Sondermann, D.Bar-Sagi, and J.Kuriyan (2010).
Role of the histone domain in the autoinhibition and activation of the Ras activator Son of Sevenless.
  Proc Natl Acad Sci U S A, 107, 3430-3435.
PDB code: 3ksy
18454158 J.Gureasko, W.J.Galush, S.Boykevisch, H.Sondermann, D.Bar-Sagi, J.T.Groves, and J.Kuriyan (2008).
Membrane-dependent signal integration by the Ras activator Son of sevenless.
  Nat Struct Mol Biol, 15, 452-461.  
18541156 L.Buday, and J.Downward (2008).
Many faces of Ras activation.
  Biochim Biophys Acta, 1786, 178-187.  
17215368 K.J.Hwang, F.Mahmoodian, J.A.Ferretti, E.D.Korn, and J.M.Gruschus (2007).
Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.
  Proc Natl Acad Sci U S A, 104, 784-789.  
16267129 H.Sondermann, B.Nagar, D.Bar-Sagi, and J.Kuriyan (2005).
Computational docking and solution x-ray scattering predict a membrane-interacting role for the histone domain of the Ras activator son of sevenless.
  Proc Natl Acad Sci U S A, 102, 16632-16637.  
12637530 E.J.Fuentes, A.E.Karnoub, M.A.Booden, C.J.Der, and S.L.Campbell (2003).
Critical role of the pleckstrin homology domain in Dbs signaling and growth regulation.
  J Biol Chem, 278, 21188-21196.  
11889037 K.L.Rossman, D.K.Worthylake, J.T.Snyder, D.P.Siderovski, S.L.Campbell, and J.Sondek (2002).
A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange.
  EMBO J, 21, 1315-1326.
PDB codes: 1kz7 1kzg
12223473 R.Jorge, N.Zarich, J.L.Oliva, M.Azañedo, N.Martínez, la Cruz, and J.M.Rojas (2002).
HSos1 contains a new amino-terminal regulatory motif with specific binding affinity for its pleckstrin homology domain.
  J Biol Chem, 277, 44171-44179.  
10940243 J.H.Hurley, and S.Misra (2000).
Signaling and subcellular targeting by membrane-binding domains.
  Annu Rev Biophys Biomol Struct, 29, 49-79.  
11080629 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.
  Structure, 8, 1079-1087.
PDB code: 1fho
10497244 A.D.Ma, and C.S.Abrams (1999).
Pleckstrin induces cytoskeletal reorganization via a Rac-dependent pathway.
  J Biol Chem, 274, 28730-28735.  
10393272 L.Buday (1999).
Membrane-targeting of signalling molecules by SH2/SH3 domain-containing adaptor proteins.
  Biochim Biophys Acta, 1422, 187-204.  
10542412 N.Blomberg, E.Baraldi, M.Nilges, and M.Saraste (1999).
The PH superfold: a structural scaffold for multiple functions.
  Trends Biochem Sci, 24, 441-445.  
10591098 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.
  Proteins, 37, 379-387.  
  9671484 A.D.Ma, A.Metjian, S.Bagrodia, S.Taylor, and C.S.Abrams (1998).
Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase gamma, a Rac guanosine exchange factor, and Rac.
  Mol Cell Biol, 18, 4744-4751.  
9438849 A.S.Nimnual, B.A.Yatsula, and D.Bar-Sagi (1998).
Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos.
  Science, 279, 560-563.  
9846881 B.Aghazadeh, K.Zhu, T.J.Kubiseski, G.A.Liu, T.Pawson, Y.Zheng, and M.K.Rosen (1998).
Structure and mutagenesis of the Dbl homology domain.
  Nat Struct Biol, 5, 1098-1107.
PDB code: 1by1
9813005 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.
  J Biol Chem, 273, 31061-31067.  
9838087 D.R.Alessi, and C.P.Downes (1998).
The role of PI 3-kinase in insulin action.
  Biochim Biophys Acta, 1436, 151-164.  
9593218 M.Hirata, T.Kanematsu, H.Takeuchi, and H.Yagisawa (1998).
Pleckstrin homology domain as an inositol compound binding module.
  Jpn J Pharmacol, 76, 255-263.  
9838094 M.J.Bottomley, K.Salim, and G.Panayotou (1998).
Phospholipid-binding protein domains.
  Biochim Biophys Acta, 1436, 165-183.  
9646876 M.J.Rebecchi, and S.Scarlata (1998).
Pleckstrin homology domains: a common fold with diverse functions.
  Annu Rev Biophys Biomol Struct, 27, 503-528.  
9736615 S.J.Isakoff, T.Cardozo, J.Andreev, Z.Li, K.M.Ferguson, R.Abagyan, M.A.Lemmon, A.Aronheim, and E.Y.Skolnik (1998).
Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast.
  EMBO J, 17, 5374-5387.  
9374522 J.Zheng, R.H.Chen, S.Corblan-Garcia, S.M.Cahill, D.Bar-Sagi, and D.Cowburn (1997).
The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains.
  J Biol Chem, 272, 30340-30344.
PDB code: 1awe
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