Direct Photoaffinity Labeling of Cellular Retinoic Acid-Binding Protein I (CRABP-I) withall-trans-Retinoic Acid:  Identification of Amino Acids in the Ligand Binding Site†

Biochemistry ◽  
2000 ◽  
Vol 39 (41) ◽  
pp. 12568-12574 ◽  
Author(s):  
Guangping Chen ◽  
Anna Radominska-Pandya
Keyword(s):  
Amino Acids ◽  
Retinoic Acid ◽  
Ligand Binding ◽  
Binding Site ◽  
Binding Protein ◽  
Photoaffinity Labeling ◽  
Ligand Binding Site ◽  
Acid Binding Protein ◽  
Trans Retinoic Acid ◽  
Crabp I

NMR Solution Structure of Type II Human Cellular Retinoic Acid Binding Protein:  Implications for Ligand Binding†,‡

Biochemistry ◽  
1998 ◽  
Vol 37 (37) ◽  
pp. 12727-12736 ◽  
Author(s):  
Lincong Wang ◽  
Yue Li ◽  
Frits Abildgaard ◽  
John L. Markley ◽  
Honggao Yan
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Solution Structure ◽  
Binding Protein ◽  
Type Ii ◽  
Nmr Solution Structure ◽  
Acid Binding Protein

scholarly journals Modification of the loops in the ligand-binding site turns avidin into a steroid-binding protein

2011 ◽  
Vol 11 (1) ◽  
pp. 64 ◽  
Author(s):  
Tiina A Riihimäki ◽  
Soili Hiltunen ◽  
Martina Rangl ◽  
Henri R Nordlund ◽  
Juha AE Määttä ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Binding Protein ◽  
Ligand Binding Site ◽  
Steroid Binding ◽  
Steroid Binding Protein

Domains of cellular retinoic acid-binding protein I (CRABP I) expression in the hindbrain and neural crest of the mouse embryo

1992 ◽  
Vol 37 (1-2) ◽  
pp. 13-23 ◽  
Author(s):  
Malcolm Maden ◽  
Claire Horton ◽  
Anthony Graham ◽  
Lisa Leonard ◽  
John Pizzey ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Neural Crest ◽  
Mouse Embryo ◽  
Binding Protein ◽  
Acid Binding Protein ◽  
Crabp I

Structural Determinants of the Ligand-Binding Site of the Human Retinoic Acid Receptor .alpha.

Biochemistry ◽  
1995 ◽  
Vol 34 (16) ◽  
pp. 5477-5485 ◽  
Author(s):  
Bruno Lefebvre ◽  
Christophe Rachez ◽  
Pierre Formstecher ◽  
Philippe Lefebvre
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Binding Site ◽  
Retinoic Acid Receptor ◽  
Ligand Binding Site ◽  
Retinoic Acid Receptor Alpha ◽  
Structural Determinants ◽  
Acid Receptor ◽  
Receptor Alpha

Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation

2009 ◽  
Vol 390 (11) ◽  
Author(s):  
Christine Oswald ◽  
Sander H.J. Smits ◽  
Marina Höing ◽  
Erhard Bremer ◽  
Lutz Schmitt
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Ligand Binding ◽  
Closed Form ◽  
Binding Site ◽  
Sinorhizobium Meliloti ◽  
Binding Protein ◽  
Ligand Binding Site ◽  
Abc Transport ◽  
Ligand Free

Abstract The periplasmic ligand-binding protein ChoX is part of the ABC transport system ChoVWX that imports choline as a nutrient into the soil bacterium Sinorhizobium meliloti. We have recently reported the crystal structures of ChoX in complex with its ligands choline and acetylcholine and the structure of a fully closed but substrate-free state of ChoX. This latter structure revealed an architecture of the ligand-binding site that is superimposable to the closed, ligand-bound form of ChoX. We report here the crystal structure of ChoX in an unusual, ligand-free conformation that represents a semi-closed form of ChoX. The analysis revealed a subdomain movement in the N-lobe of ChoX. Comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.

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