scholarly journals The High Affinity Ligand Binding Conformation of the Nuclear 1,25-dihydroxyvitamin D3 Receptor is Functionally Linked to the Transactivation Domain 2 (AF-2)

1996 ◽  
Vol 24 (22) ◽  
pp. 4513-4518 ◽  
Author(s):  
S. Nayeri ◽  
J.-P. Kahlen ◽  
C. Carlberg
Keyword(s):  
Ligand Binding ◽  
Transactivation Domain ◽  
D3 Receptor ◽  
Dihydroxyvitamin D3 ◽  
High Affinity ◽  
Binding Conformation ◽  
1,25 Dihydroxyvitamin D3 ◽  
Affinity Ligand ◽  
High Affinity Ligand

scholarly journals High Affinity Ligand Binding by Integrins Does Not Involve Head Separation

2003 ◽  
Vol 278 (19) ◽  
pp. 17185-17189 ◽  
Author(s):  
Bing-Hao Luo ◽  
Timothy A. Springer ◽  
Junichi Takagi
Keyword(s):  
Ligand Binding ◽  
High Affinity ◽  
Affinity Ligand ◽  
High Affinity Ligand

scholarly journals Rat and human neutrophil N-formyl-peptide chemotactic receptors. Species difference in the glycosylation of similar 35-38 kDa polypeptide cores

1991 ◽  
Vol 277 (1) ◽  
pp. 67-72 ◽  
Author(s):  
J J Remes ◽  
U E Petäjä-Repo ◽  
H J Rajaniemi
Keyword(s):  
Ligand Binding ◽  
Species Difference ◽  
Cross Linking ◽  
Complex Type ◽  
High Affinity ◽  
Affinity Ligand ◽  
Pngase F ◽  
Formyl Peptide ◽  
Membrane Bound ◽  
High Affinity Ligand

Rat and human neutrophil N-formyl-peptide chemotactic receptors were subjected to glycosidase and proteinase treatments to determine the extent and species differences of glycosylation and the carbohydrate requirement in the high-affinity ligand binding. N-Formyl-Nle-Leu-Phe-Nle-125I-Tyr-Lys was attached to rat and human neutrophils either before or after glycosidase and proteinase treatments, and the labelled receptors were solubilized after glutaraldehyde cross-linking and analysed by SDS/PAGE and autoradiography. Both the rat and human N-formyl-peptide chemotactic receptors contain only N-linked oligosaccharides, as demonstrated by their sensitivity to peptide N-glycosidase F (PNGase F) and resistance to O-glycanase treatment. The N-linked oligosaccharides seem to be of the complex type rather than the high-mannose or hybrid type and lack terminal sialic acid, as demonstrated by their resistance to endoglycosidases D and H and neuraminidase treatments. This sensitivity pattern was similar in both species, and the shift in the molecular size of the receptors to 35-38 kDa after PNGase F treatment occurred through one intermediate product, suggesting that both receptors contain a similar 35-38 kDa polypeptide core with two N-linked complex-type oligosaccharides, the heterogeneity of which is responsible for the species difference in receptor size. Papain treatment alone or followed by PNGase F produced in both species a 33-36 kDa membrane-bound fragment that was still able to bind the ligand, suggesting that the oligosaccharides are located on the approx. 2 kDa papain-cleavable polypeptide fragment of the receptors. The cleavage sites for both papain and PNGase F were hidden in occupied receptors, suggesting a conformational or topographical change in these upon ligand binding. Scatchard analyses and cross-linking experiments demonstrated that carbohydrates are not required for high-affinity ligand binding and that the 33-36 kDa membrane-bound papain fragment of both receptors contains the ligand-binding site.

ChemInform Abstract: Design and Synthesis of 2α-(Tetrazolylethyl)-1α,25-dihydroxyvitamin D3 as a High Affinity Ligand for Vitamin D Receptor

ChemInform ◽  
2015 ◽  
Vol 46 (9) ◽  
pp. no-no
Author(s):  
Miki Matsuo ◽  
Asami Hasegawa ◽  
Masashi Takano ◽  
Hiroshi Saito ◽  
Shinji Kakuda ◽  
...  
Keyword(s):  
Vitamin D ◽  
Vitamin D Receptor ◽  
Dihydroxyvitamin D3 ◽  
Design And Synthesis ◽  
High Affinity ◽  
Affinity Ligand ◽  
High Affinity Ligand
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