scholarly journals Methionine acts as a “magnet” in photoaffinity crosslinking experiments

FEBS Letters ◽  
2006 ◽  
Vol 580 (7) ◽  
pp. 1872-1876 ◽  
Author(s):  
Angela Wittelsberger ◽  
Beena E. Thomas ◽  
Dale F. Mierke ◽  
Michael Rosenblatt
Keyword(s):  
Photoaffinity Crosslinking

Identification of the A2 Adenosine Receptor Binding Subunit by Photoaffinity Crosslinking

1990 ◽  
pp. 82-85
Author(s):  
W. W. Barrington ◽  
K. A. Jacobson ◽  
A. J. Hutchison ◽  
M. Williams ◽  
G. L. Stiles
Keyword(s):  
Receptor Binding ◽  
Adenosine Receptor ◽  
Photoaffinity Crosslinking ◽  
Binding Subunit

scholarly journals Identification and characterization of the rat adipocyte glucose transporter by photoaffinity crosslinking

FEBS Letters ◽  
1983 ◽  
Vol 164 (2) ◽  
pp. 261-266 ◽  
Author(s):  
Richard Horuk ◽  
Martin Rodbell ◽  
Samuel W. Cushman ◽  
Ian A. Simpson
Keyword(s):  
Glucose Transporter ◽  
Identification And Characterization ◽  
Photoaffinity Crosslinking

scholarly journals Hedgehog proteins create a dynamic cholesterol interface

PLoS ONE ◽  
2021 ◽  
Vol 16 (2) ◽  
pp. e0246814 ◽  
Author(s):  
Amirhossein Mafi ◽  
Rahul Purohit ◽  
Erika Vielmas ◽  
Alexa R. Lauinger ◽  
Brandon Lam ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Sonic Hedgehog ◽  
Tissue Regeneration ◽  
Molecular Basis ◽  
Signaling Proteins ◽  
Full Structure ◽  
Hedgehog Proteins ◽  
Hh Signaling ◽  
Dynamics Simulations ◽  
Photoaffinity Crosslinking

During formation of the Hedgehog (Hh) signaling proteins, cooperative activities of the Hedgehog INTein (Hint) fold and Sterol Recognition Region (SRR) couple autoproteolysis to cholesterol ligation. The cholesteroylated Hh morphogens play essential roles in embryogenesis, tissue regeneration, and tumorigenesis. Despite the centrality of cholesterol in Hh function, the full structure of the Hint-SRR (“Hog”) domain that attaches cholesterol to the last residue of the active Hh morphogen remains enigmatic. In this work, we combine molecular dynamics simulations, photoaffinity crosslinking, and mutagenesis assays to model cholesterolysis intermediates in the human Sonic Hedgehog (hSHH) protein. Our results provide evidence for a hydrophobic Hint-SRR interface that forms a dynamic, non-covalent cholesterol-Hog complex. Using these models, we suggest a unified mechanism by which Hh proteins can recruit, sequester, and orient cholesterol, and offer a molecular basis for the effects of disease-causing hSHH mutations.

scholarly journals Analysis of the conformation of the 3′ major domain of Escherichia coli 16S ribosomal RNA using site-directed photoaffinity crosslinking

RNA ◽  
1998 ◽  
Vol 4 (11) ◽  
pp. 1455-1466 ◽  
Author(s):  
ALEXANDRE MONTPETIT ◽  
CATHERINE PAYANT ◽  
JAMES M. NOLAN ◽  
LÉA BRAKIER-GINGRAS
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
16S Ribosomal Rna ◽  
Photoaffinity Crosslinking ◽  
Major Domain
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