More meanders and sandwiches

@article{Riddihough1994MoreMA,
  title={More meanders and sandwiches},
  author={Guy Riddihough},
  journal={Nature Structural Biology},
  year={1994},
  volume={1},
  pages={755-757}
}
  • G. Riddihough
  • Published 1 November 1994
  • Engineering
  • Nature Structural Biology
As investigations into the structure and function of the PH domain intensify there are no shortage of clues as to the role of this domain in signal transduction, and yet the physiological ligand remains elusive. 
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12 Citations
Background Citations
4
Methods Citations
1

12 Citations

Citation Type

Citation Type

Scratching the surface with the PH domain
TLDR
Recent structural studies provide a model for PH domain anchoring to inositol phospholipids that will open new avenues for functional investigation.
Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
The structure of the putative membrane-binding tandem PX-PH domain module of the yeast protein Bem3 is reported.
Structural similarity between the pleckstrin homology domain and verotoxin: The problem of measuring and evaluating structural similarity
An unexpected structural similarity is described between the pleckstrin homology (PH) domain and verotoxin. This similarity has escaped detection primarily due to the differences in topology that…
Pleckstrin homology domains: a fact file.
Folded and Unfolded Conformations of Proteins Involved in Pancreatic Cancer: a Layman's Guide
TLDR
It is shown not only that well-folded proteins in several signaling pathways are critical in the development of PC, but also that natively unfolded “hub” proteins, able to interact with DNA or proteins, are also important in such cancer progression.
Specialized structural and functional roles of residues selectively conserved in subfamilies of the pleckstrin homology domain family
TLDR
DA‐specific residues in PH domain are found to contribute to structural and functional specialization of ARNO and GRK2 in terms of specific intra‐ and interprotein interactions; specificity for phospholipids; and participation in conformational excursions, leading to various functional forms.
Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization.
Protein modules and signalling networks
TLDR
This work highlights conserved protein domains that act as key regulatory participants in many of these different signalling pathways in multicellular organisms.
Differential Lipid Binding Properties and Physiological Functions of Sorting Nexin Family Proteins
TLDR
This new discovery suggests that SNX21 is a novel dual specificity protein that can interact with both membrane lipids and nucleic acids and that it may serve as a new class of endonuclease that plays a role in apoptosis.
PDGF and FGF receptors in health and disease
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References

SHOWING 1-10 OF 12 REFERENCES
Thin end of the wedge
  • G. Wagner
  • Chemistry
    Nature Structural Biology
  • 1994
The principle fold of the pleckstrin homology domain, found in a subset of cytoskeletal and signal transduction proteins, is now revealed and will inform and direct functional studies.
Crystal structure of the pleckstrin homology domain from dynamin
TLDR
The 2.8 Å crystal structure of the PH domain from dynamin consists of seven β-strands forming two roughly orthogonal antiparallel β-sheets terminating with an amphipathic α-helix and reveals a non-covalent dimeric association of thePH domain and a hydrophobic pocket surrounded by a charged rim.
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.
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.
Three-dimensional solution structure of the pleckstrin homology domain from dynamin
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.
The PH domain: a common piece in the structural patchwork of signalling proteins.
Structural requirements of phosphatidylinositol‐specific phospholipase C δ1 for enzyme activity
TLDR
Using a combination of deletion mutant analysis and limited proteolysis, it was found that the large proportion of the molecule participated in formation of a catalytic domain and included regions of high and low conservation with other phospholipase-C molecules.
Proteolytic fragments of phosphoinositide-specific phospholipase C-delta 1. Catalytic and membrane binding properties.
Interaction of dynamin with microtubules: its structure and GTPase activity investigated by using highly purified dynamin.
TLDR
Despite slow GTPase turnover rate in the absence of microtubules, binding of GTP and its nonhydrolizing analogues was very fast, indicating that GTP binding step is not rate limiting.
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