Definition of peptide binding motifs amongst the HLA-A*30 allelic group

2000 ◽  
Vol 56 (1) ◽  
pp. 10-18 ◽  
Author(s):  
P. Krausa ◽  
C. Münz ◽  
W. Keilholz ◽  
S. Stevanovic ◽  
E.Y. Jones ◽  
...  
Keyword(s):  
Peptide Binding ◽  
Binding Motifs ◽  
Allelic Group ◽  
Definition Of

scholarly journals Identification of Five Different Patr Class I Molecules That Bind HLA Supertype Peptides and Definition of Their Peptide Binding Motifs

2000 ◽  
Vol 165 (8) ◽  
pp. 4414-4422 ◽  
Author(s):  
Denise M. McKinney ◽  
Ann L. Erickson ◽  
Christopher M. Walker ◽  
Robert Thimme ◽  
Francis V. Chisari ◽  
...  
Keyword(s):  
Peptide Binding ◽  
Class I ◽  
Binding Motifs ◽  
Definition Of

Barcoded Rational AAV Vector Evolution Enables Systematic In Vivo Mapping of Peptide Binding Motifs

2018 ◽  
Author(s):  
Marcus Davidsson ◽  
Gang Wang ◽  
Patrick Aldrin-Kirk ◽  
Tiago Cardoso ◽  
Sara Nolbrant ◽  
...  
Keyword(s):  
Peptide Binding ◽  
Aav Vector ◽  
Binding Motifs

scholarly journals Peptide-binding motifs associated with MHC molecules common in Chinese rhesus macaques are analogous to those of human HLA supertypes and include HLA-B27-like alleles

2013 ◽  
Vol 65 (5) ◽  
pp. 371-386 ◽  
Author(s):  
Bianca R. Mothé ◽  
Scott Southwood ◽  
John Sidney ◽  
A. Michelle English ◽  
Amanda Wriston ◽  
...  
Keyword(s):  
Rhesus Macaques ◽  
Peptide Binding ◽  
Hla B27 ◽  
Binding Motifs ◽  
Mhc Molecules ◽  
Chinese Rhesus Macaques

scholarly journals Direct visualization of interaction between calmodulin and connexin45

2017 ◽  
Vol 474 (24) ◽  
pp. 4035-4051 ◽  
Author(s):  
Juan Zou ◽  
Mani Salarian ◽  
Yanyi Chen ◽  
You Zhuo ◽  
Nicole E. Brown ◽  
...  
Keyword(s):  
Peptide Binding ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Direct Interaction ◽  
Resonance Spectroscopy ◽  
Direct Visualization ◽  
Bioluminescence Resonance Energy Transfer ◽  
Binding Motifs ◽  
Physiological Conditions ◽  
Interaction Mode

Calmodulin (CaM) is an intracellular Ca2+ transducer involved in numerous activities in a broad Ca2+ signaling network. Previous studies have suggested that the Ca2+/CaM complex may participate in gap junction regulation via interaction with putative CaM-binding motifs in connexins; however, evidence of direct interactions between CaM and connexins has remained elusive to date due to challenges related to the study of membrane proteins. Here, we report the first direct interaction of CaM with Cx45 (connexin45) of γ-family in living cells under physiological conditions by monitoring bioluminescence resonance energy transfer. The interaction between CaM and Cx45 in cells is strongly dependent on intracellular Ca2+ concentration and can be blocked by the CaM inhibitor, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide hydrochloride (W7). We further reveal a CaM-binding site at the cytosolic loop (residues 164–186) of Cx45 using a peptide model. The strong binding (Kd ∼ 5 nM) observed between CaM and Cx45 peptide, monitored by fluorescence-labeled CaM, is found to be Ca2+-dependent. Furthermore, high-resolution nuclear magnetic resonance spectroscopy reveals that CaM and Cx45 peptide binding leads to global chemical shift changes of 15N-labeled CaM, but does not alter the size of the structure. Observations involving both N- and C-domains of CaM to interact with the Cx45 peptide differ from the embraced interaction with Cx50 from another connexin family. Such interaction further increases Ca2+ sensitivity of CaM, especially at the N-terminal domain. Results of the present study suggest that both helicity and the interaction mode of the cytosolic loop are likely to contribute to CaM's modulation of connexins.

Cell-Specific Peptide Binding by Human Neutrophils

Blood ◽  
1999 ◽  
Vol 93 (5) ◽  
pp. 1738-1748
Author(s):  
Luca Mazzucchelli ◽  
James B. Burritt ◽  
Algirdas J. Jesaitis ◽  
Asma Nusrat ◽  
Tony W. Liang ◽  
...  
Keyword(s):  
Specific Binding ◽  
Peptide Binding ◽  
Cytosolic Calcium ◽  
Human Neutrophils ◽  
High Avidity ◽  
Binding Motifs ◽  
Diagnostic Strategies ◽  
Ionic Detergent ◽  
Normal Human ◽  
Phage Libraries

Analysis of peptide binding to human neutrophils (PMN) using phage display techniques has revealed cell-specific motifs reactive with the PMN surface. Phage libraries displaying either linear 9-mer or cyclic 10-mer and 6-mer peptides were incubated with normal human neutrophils followed by elution of bound phage with low pH (pH 2.2) and non-ionic detergent. Three rounds of selection generated several related peptide sequences that bound with high avidity to PMN. Using the linear 9-mer library, PMN-binding phage expressed peptides with the motif (G/A)PNLTGRW. The binding of phage bearing this motif was highly specific since no binding was observed on lymphocytes, fibroblasts, epithelial, or endothelial cells. Functional assays revealed that phage bearing the sequence FGPNLTGRW induced a pertussis toxin-sensitive increase in PMN cytosolic calcium analogous to that observed with Gi coupled receptors. Other prominent motifs identified included phage bearing the consensus DLXTSK(M/L)X(V/I/L), where X represents a non-conserved position. Phage with this motif bound exclusively to a sub population of human PMN that comprised approximately 50% of the total and did not elicit a calcium response. The binding of such phage to PMN was prevented by co-incubation with competing peptides displaying identical or similar sequences (IC50 range from 0.6 μmol/L to 50 μmol/L for DLXTSK and GPNLTG, respectively). We speculate that these techniques will be useful in identifying functional cell-specific binding motifs and contribute to the development of new therapeutic and diagnostic strategies in human disease.

scholarly journals Structure of Pumilio Reveals Similarity between RNA and Peptide Binding Motifs

Cell ◽  
2001 ◽  
Vol 105 (2) ◽  
pp. 281-289 ◽  
Author(s):  
Thomas A Edwards ◽  
Scott E Pyle ◽  
Robin P Wharton ◽  
Aneel K Aggarwal
Keyword(s):  
Peptide Binding ◽  
Binding Motifs
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