Control of Protein−Protein Interactions:  Structure-Based Discovery of Low Molecular Weight Inhibitors of the Interactions between Pin1 WW Domain and Phosphopeptides

2005 ◽  
Vol 48 (15) ◽  
pp. 4815-4823 ◽  
Author(s):  
Caroline Smet ◽  
Jean-Frédéric Duckert ◽  
Jean-Michel Wieruszeski ◽  
Isabelle Landrieu ◽  
Luc Buée ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Interactions ◽  
Low Molecular Weight ◽  
Protein Protein Interactions ◽  
Ww Domain

Low-molecular-weight spies of protein–protein interactions

2008 ◽  
Vol 11 (4-5) ◽  
pp. 499-505 ◽  
Author(s):  
Jascha Blobel ◽  
Rosa Fayos ◽  
Jesús García ◽  
Oriol Marimon ◽  
Yolanda Pérez ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Interactions ◽  
Low Molecular Weight ◽  
Protein Protein Interactions

scholarly journals Set-up and screening of a fragment library targeting the 14-3-3 protein interface

MedChemComm ◽  
2019 ◽  
Vol 10 (10) ◽  
pp. 1796-1802 ◽  
Author(s):  
Dario Valenti ◽  
João Filipe Neves ◽  
François-Xavier Cantrelle ◽  
Stanimira Hristeva ◽  
Domenico Lentini Santo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Interactions ◽  
Low Molecular Weight ◽  
Protein Interface ◽  
Protein Protein Interactions ◽  
Fragment Library ◽  
Set Up

Fragment-based driven discovery of 3 new low molecular weight starting points for the modulation of 14-3-3 protein–protein interactions.

PHYSICOCHEMICAL PROPERTIES OF S-ZONE AND BASE PROTEINS IN GLUTEN

1966 ◽  
Vol 44 (6) ◽  
pp. 917-925 ◽  
Author(s):  
Yang H. Oh ◽  
Benjamin E. Sanders ◽  
Charles W. Gehrke
Keyword(s):  
Amino Acid ◽  
Physicochemical Properties ◽  
Protein Interactions ◽  
Wheat Gluten ◽  
Amino Acid Content ◽  
Low Molecular Weight ◽  
Protein Protein Interactions ◽  
Contributing Factors ◽  
Protein Molecules ◽  
Stable Structures

Some of the physicochemical properties (solubility, viscosity, sedimentation) and the amino acid composition of the isolated S-zone and base proteins from soft-wheat gluten were studied. The S-zone proteins are homogeneous in size, of low molecular weight (about 20,000), and high intrinsic viscosity in buffer of pH 3,5, having stable structures whose unique solubility properties are related to their atypical amino acid content. The base protein molecules exist in a more folded conformation, having the properties of globular protein molecules. The protein–protein interactions, aggregation, and unfolding conformation of S-zone proteins are major contributing factors at neutral pH to the rheological properties of wheat flour, such as viscosity, elasticity, and cohesiveness.

scholarly journals TraC of IncN Plasmid pKM101 Associates with Membranes and Extracellular High-Molecular-Weight Structures inEscherichia coli

1999 ◽  
Vol 181 (18) ◽  
pp. 5563-5571 ◽  
Author(s):  
Heike Schmidt-Eisenlohr ◽  
Natalie Domke ◽  
Christian Baron
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Protein Interactions ◽  
Dna Transfer ◽  
Protein Protein Interactions ◽  
High Molecular Weight Complex ◽  
Plasmid Pkm101 ◽  
Transposon Insertions ◽  
Transfer Apparatus ◽  
Weight Structures

ABSTRACT Conjugative transfer of IncN plasmid pKM101 is mediated by the TraI-TraII region-encoded transfer machinery components. Similar to the case for the related Agrobacterium tumefaciens T-complex transfer apparatus, this machinery is needed for assembly of pili to initiate cell-to-cell contact preceding DNA transfer. Biochemical and cell biological experiments presented here show extracellular localization of TraC, as suggested by extracellular complementation of TraC-deficient bacteria by helper cells expressing a functional plasmid transfer machinery (S. C. Winans, and G. C. Walker, J. Bacteriol. 161:402–410, 1985). Overexpression of TraC and its export in large amounts into the periplasm of Escherichia coliallowed purification by periplasmic extraction, ammonium sulfate precipitation, and column chromatography. Whereas TraC was soluble in overexpressing strains, it partly associated with the membranes in pKM101-carrying cells, possibly due to protein-protein interactions with other components of the TraI-TraII region-encoded transfer machinery. Membrane association of TraC was reduced in strains carrying pKM101 derivatives with transposon insertions in genes coding for other essential components of the transfer machinery,traM, traB, traD, andtraE but not eex, coding for an entry exclusion protein not required for DNA transfer. Cross-linking identified protein-protein interactions of TraC in E. coli carrying pKM101 but not derivatives with transposon insertions in essentialtra genes. Interactions with membrane-bound Tra proteins may incorporate TraC into a surface structure, suggested by its removal from the cell by shearing as part of a high-molecular-weight complex. Heterologous expression of TraC in A. tumefaciens partly compensated for the pilus assembly defect in strains deficient for its homolog VirB5, which further supported its role in assembly of conjugative pili. In addition to its association with high-molecular-weight structures, TraC was secreted into the extracellular milieu. Conjugation experiments showed that secreted TraC does not compensate transfer deficiency of TraC-deficient cells, suggesting that extracellular complementation may rely on cell-to-cell transfer of TraC only as part of a bona fide transfer apparatus.

scholarly journals WWOX-Mediated Degradation of AMOTp130 Negatively Affects Egress of Filovirus VP40 VLPs

2021 ◽  
Author(s):  
Jingjing Liang ◽  
Gordon Ruthel ◽  
Bruce Freedman ◽  
Ronald N. Harty
Keyword(s):  
Protein Interactions ◽  
Matrix Protein ◽  
Host Protein ◽  
Hemorrhagic Disease ◽  
Protein Protein Interactions ◽  
Virus Budding ◽  
Ww Domain ◽  
Virion Assembly ◽  
Domain Interactions ◽  
Virus Egress

Ebola (EBOV) and Marburg (MARV) viruses continue to emerge and cause severe hemorrhagic disease in humans. A comprehensive understanding of the filovirus-host interplay will be crucial for identifying and developing antiviral strategies. The filoviral VP40 matrix protein drives virion assembly and egress, in part by recruiting specific WW-domain-containing host interactors via its conserved PPxY Late (L) domain motif to positively regulate virus egress and spread. In contrast to these positive regulators of virus budding, a growing list of WW-domain-containing interactors that negatively regulate virus egress and spread have been identified, including BAG3, YAP/TAZ and WWOX. In addition to host WW-domain regulators of virus budding, host PPxY-containing proteins also contribute to regulating this late stage of filovirus replication. For example, angiomotin (AMOT) is a multi-PPxY-containing host protein that functionally interacts with many of the same WW-domain-containing proteins that regulate virus egress and spread. In this report, we demonstrate that host WWOX, which negatively regulates egress of VP40 VLPs and recombinant VSV-M40 virus, interacts with and suppresses the expression of AMOT. We found that WWOX disrupts AMOT’s scaffold-like tubular distribution and reduces AMOT localization at the plasma membrane via lysosomal degradation. In sum, our findings reveal an indirect and novel mechanism by which modular PPxY/WW-domain interactions between AMOT and WWOX regulate PPxY-mediated egress of filovirus VP40 VLPs. A better understanding of this modular network and competitive nature of protein-protein interactions will help to identify new antiviral targets and therapeutic strategies.

Sign in / Sign up

Export Citation Format

Share Document