Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein

2008 ◽  
Vol 21 (5) ◽  
pp. 348-354 ◽  
Author(s):  
Piero Ricchiuto ◽  
Alessandro Guerini Rocco ◽  
Elisabetta Gianazza ◽  
Dario Corrada ◽  
Tiziana Beringhelli ◽  
...  
2008 ◽  
Vol 71 (4) ◽  
pp. 1889-1898 ◽  
Author(s):  
Ivano Eberini ◽  
Alessandro Guerini Rocco ◽  
Anna Rita Ientile ◽  
António M. Baptista ◽  
Elisabetta Gianazza ◽  
...  

2006 ◽  
Vol 281 (14) ◽  
pp. 9697-9709 ◽  
Author(s):  
Laura Ragona ◽  
Maddalena Catalano ◽  
Marianna Luppi ◽  
Daniel Cicero ◽  
Tommaso Eliseo ◽  
...  

Biochemistry ◽  
2005 ◽  
Vol 44 (23) ◽  
pp. 8486-8493 ◽  
Author(s):  
Verónica Nolan ◽  
Massimiliano Perduca ◽  
Hugo L. Monaco ◽  
Guillermo G. Montich

Biochemistry ◽  
2007 ◽  
Vol 46 (44) ◽  
pp. 12557-12567 ◽  
Author(s):  
Tommaso Eliseo ◽  
Laura Ragona ◽  
Maddalena Catalano ◽  
Michael Assfalg ◽  
Maurizio Paci ◽  
...  

2007 ◽  
Vol 69 (1) ◽  
pp. 177-191 ◽  
Author(s):  
Simona Tomaselli ◽  
Laura Ragona ◽  
Lucia Zetta ◽  
Michael Assfalg ◽  
Pasquale Ferranti ◽  
...  

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 645
Author(s):  
Giusy Tassone ◽  
Maurizio Orlandini ◽  
Massimo Olivucci ◽  
Cecilia Pozzi

Bile acids (BAs) are hydroxylated steroids derived from cholesterol that act at the intestinal level to facilitate the absorption of several nutrients and also play a role as signaling molecules. In the liver of various vertebrates, the trafficking of BAs is mediated by bile acid-binding proteins (L-BABPs). The ability to host hydrophobic or amphipathic molecules makes BABPs suitable for the distribution of a variety of physiological and exogenous substances. Thus, BABPs have been proposed as drug carriers, and more recently, they have also been employed to develop innovative nanotechnology and biotechnology systems. Here, we report an efficient protocol for the production, purification, and crystallization of chicken liver BABP (cL-BABP). By means of target expression as His6-tag cL-BABP, we obtained a large amount of pure and homogeneous proteins through a simple purification procedure relying on affinity chromatography. The recombinant cL-BABP showed a raised propensity to crystallize, allowing us to obtain its structure at high resolution and, in turn, assess the structural conservation of the recombinant cL-BABP with respect to the liver-extracted protein. The results support the use of recombinant cL-BABP for the development of drug carriers, nanotechnologies, and innovative synthetic photoswitch systems.


2009 ◽  
Vol 481 (1) ◽  
pp. 21-29 ◽  
Author(s):  
Mariapina D’Onofrio ◽  
Laura Ragona ◽  
Dimitrios Fessas ◽  
Marco Signorelli ◽  
Raffaella Ugolini ◽  
...  

1999 ◽  
Vol 274 (42) ◽  
pp. 29749-29754 ◽  
Author(s):  
Jacques Grober ◽  
Isabelle Zaghini ◽  
Hiroshi Fujii ◽  
Stacey A. Jones ◽  
Steven A. Kliewer ◽  
...  

2019 ◽  
Vol 10 (9) ◽  
pp. 2235-2243 ◽  
Author(s):  
Katiuscia Pagano ◽  
Marco Paolino ◽  
Stefania Fusi ◽  
Vinicio Zanirato ◽  
Claudio Trapella ◽  
...  

FEBS Journal ◽  
2016 ◽  
Vol 283 (3) ◽  
pp. 541-555 ◽  
Author(s):  
Gergő Horváth ◽  
Ákos Bencsura ◽  
Ágnes Simon ◽  
Gregory P. Tochtrop ◽  
Gregory T. DeKoster ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document