The PH domain: a common piece in the structural patchwork of signalling proteins.

@article{Musacchio1993ThePD,
  title={The PH domain: a common piece in the structural patchwork of signalling proteins.},
  author={Andrea Musacchio and Toby J. Gibson and P A Rice and J Drew Thompson and Matti Saraste},
  journal={Trends in biochemical sciences},
  year={1993},
  volume={18 9},
  pages={
          343-8
        }
}
Structure of the pleckstrin homology domain from β-spectrin
TLDR
The three-dimensional structure of the PH domain of the cytoskeletal protein spectrin is reported using homonuclear nuclear magnetic resonance to report a distant relationship to the peptidyl-prolyl-cis-trans-isomerase FKBP in which this pocket is involved in the binding of the macrocyclic compound FK506.
Pleckstrin homology domain as an inositol compound binding module.
TLDR
This review focuses on membrane targeting through the binding to inositol phosphates/phosphoinositides, a region of approximately 120 amino acids that can form an electrostatically polarized tertiary structure in proteins containing the PH domain.
Interactions between Protein Kinase C and Pleckstrin Homology Domains
TLDR
The results indicate that PKC binding to PH domains involve the β2–β3 region of the Btk PH domain and the C1 region of PKC, and agents that interact with either of these regions might act to regulate PKC-PH domain binding.
Signal-dependent membrane targeting by pleckstrin homology (PH) domains.
TLDR
The possibility that membrane targeting by PH domains with low affinity for phosphoinositides could be driven by alteration of their oligomeric state and thus the avidity of their membrane binding is discussed.
Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
TLDR
It is reported that pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate and shown that the lipid-binding site is located at the lip of the β-barrel.
Pleckstrin homology domains.
TLDR
This chapter discusses the structure of PH domains, and the characteristics that make them ideally suited for binding to the membrane surface, and will consider how they may participate in defining the specificity of intermolecular interactions and compartmentalization required for the function of their host proteins in signaling processes.
Solution structure of a pleckstrin-homology domain
TLDR
The solution structure of the N-terminal pleckstrin-homology domain of pleckSTRin is determined using heteronuclear three-dimensional nuclear magnetic resonance spectroscopy and is similar to that of the retinol-binding protein family of structures.
Pleckstrin homology (PH) domains in signal transducton
TLDR
Detailed analysis indicates that the PH domain is not generally a βγ binding domain, so the race is on to find the ligands of each PH domain and determine a common nature to their interaction.
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References

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Crystal structure of a Src-homology 3 (SH3) domain
TLDR
The three-dimensional struc-ture at 1.8 Å resolution of the SH3 domain of the cytoskeletal protein spectrin expressed in Escherichia coli is reported and it is suggested that a protein ligand binds to this conserved surface of SH3.
Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.
TLDR
The 3BP-1 protein may be a mediator of SH3 function in transformation inhibition and may link tyrosine kinases to Ras-related proteins.
Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbloncogene product
TLDR
It is shown that dbl specifically catalyses the dissociation of GDP from CDC42Hsand thereby qualifies as a highly selective guanine nucleotide exchange factor for the GTP-binding protein.
Identification of a ten-amino acid proline-rich SH3 binding site.
TLDR
Identification of the SH3 binding site provides a basis for understanding the interaction between the SH2 and SH3 domains and their targets.
Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
TLDR
High-resolution crystallographic analysis of the Lck SH2 domain in complex with an 11-residue phosphopeptide derived from the hamster polyoma middle-T antigen, EPQpYEEIPIYL, shows the presence of a second pocket for the residue pY + 3 three positions C-terminal to the phosphotyrosine (pY).
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