The scFv fragment of the antibody hu4d5-8: evidence for early premature domain interaction in refolding

2001 ◽  
Vol 305 (5) ◽  
pp. 1111-1129 ◽  
Author(s):  
Marcus Jäger ◽  
Peter Gehrig ◽  
Andreas Plückthun
Keyword(s):  
Scfv Fragment ◽  
Domain Interaction

scholarly journals HIV-1 Nef Selectively Activates Src Family Kinases Hck, Lyn, and c-Src through Direct SH3 Domain Interaction

2006 ◽  
Vol 281 (37) ◽  
pp. 27029-27038 ◽  
Author(s):  
Ronald P. Trible ◽  
Lori Emert-Sedlak ◽  
Thomas E. Smithgall
Keyword(s):  
Sh3 Domain ◽  
Src Family Kinases ◽  
Domain Interaction ◽  
Hiv 1

scholarly journals Modulation of Apolipoprotein E Structure by Domain Interaction

2005 ◽  
Vol 280 (40) ◽  
pp. 34288-34295 ◽  
Author(s):  
Danny M. Hatters ◽  
Madhu S. Budamagunta ◽  
John C. Voss ◽  
Karl H. Weisgraber
Keyword(s):  
Apolipoprotein E ◽  
Domain Interaction

scholarly journals Integrative Visual Analysis of the Effects of Alternative Splicing on Protein Domain Interaction Networks

2008 ◽  
Vol 5 (2) ◽  
Author(s):  
Dorothea Emig ◽  
Melissa S. Cline ◽  
Karsten Klein ◽  
Anne Kunert ◽  
Petra Mutzel ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Protein Interactions ◽  
Visual Analysis ◽  
Protein Isoforms ◽  
Interaction Networks ◽  
Protein Domain ◽  
Domain Interaction ◽  
Exon Arrays ◽  
Exon Expression ◽  
Splicing Patterns

SummaryProteins and their interactions are essential for the functioning of all organisms and for understanding biological processes. Alternative splicing is an important molecular mechanism for increasing the protein diversity in eukaryotic cells. Splicing events that alter the protein structure and the domain composition can be responsible for the regulation of protein interactions and the functional diversity of different tissues. Discovering the occurrence of splicing events and studying protein isoforms have become feasible using Affymetrix Exon Arrays. Therefore, we have developed the versatile Cytoscape plugin DomainGraph that allows for the visual analysis of protein domain interaction networks and their integration with exon expression data. Protein domains affected by alternative splicing are highlighted and splicing patterns can be compared.

scholarly journals Formation of a complex between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Shi-qi An ◽  
Ji-liang Tang
Keyword(s):  
Virulence Factors ◽  
Xanthomonas Campestris ◽  
Adaptor Protein ◽  
Physical Interaction ◽  
Diguanylate Cyclase ◽  
Domain Interaction ◽  
Ggdef Domain ◽  
Interdomain Interactions ◽  
Xanthomonas Campestris Pv Campestris ◽  
Two Hybrid

RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris pv. campestris (Xcc), RpfG together with the sensor kinase RpfC regulates the synthesis of a range of virulence factors as a response to the cell-cell Diffusible Signaling Factor (DSF). RpfG regulates many different virulence factors by divergent pathways. Physical interaction of RpfG with two diguanylate cyclase (GGDEF) domain proteins controls motility. This is a dynamic interaction that depends upon DSF signaling and involves the conserved GYP motif in the HD-GYP domain. Here we use synthetic peptide overlay technology and yeast two-hybrid analysis in conjunction with alanine substitution mutagenesis to define a motif within the GGDEF domain proteins required for interaction. We show that regulation of motility by the GGDEF domain proteins depends upon this motif. Furthermore, we show by Y2H that both GGDEF domain proteins bind a specific PilZ domain adaptor protein, and this interacts with the pilus motor proteins PilU and PiIT. The results support a model in which DSF signaling influences motility through the interaction of proteins that affect pilus action. The motif required for HD-GYP domain interaction is conserved in a number of GGDEF domain proteins, suggesting that regulation via interdomain interactions may be of broad relevance.

A Domain Interaction Map Based on Phylogenetic Profiling

2004 ◽  
Vol 344 (5) ◽  
pp. 1331-1346 ◽  
Author(s):  
Philipp Pagel ◽  
Philip Wong ◽  
Dmitrij Frishman
Keyword(s):  
Domain Interaction ◽  
Interaction Map ◽  
Phylogenetic Profiling
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