title: Fluorescence characterization of the hydrophobic pocket of cyclophilin B.
abstract: Human cyclophilin B is a monomeric protein that contains two tryptophan residues, Trp104 and 128. Trp128-residue belongs to the binding site of cyclosporin A and is the homologous of Trp 121 in CyPA, while Trp104 residue belongs to the hydrophobic pocket. In the present work, we studied the dynamics of Trp residue(s) of cyclophilin B and of the CyPB(w128A) mutant and of TNS-mutant complex. Our results showed that Trp-104 and TNS show restricted motions within their environments and that energy transfer between the two fluorophores is occurring.
authors: Laboratoire de Biophysique Moléculaire, Université des Sciences et Technologies de Lille, Bât. C6, 59655 Villleneuve d'Ascq Cédex, France. Jihad-Rene.Albani@univ-lille1.fr
authors: J R
authors: JR
authors: Albani
authors: M
authors: M
authors: Carpentier
authors: C
authors: C
authors: Lansiaux
mesh_terms: D001665:Binding Sites; D021983:Cyclophilins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005453:Fluorescence; D005454:Fluorescence Polarization; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D009154:Mutation / Q000235:genetics; D009282:Naphthalenesulfonates / Q000737:chemistry* / Q000378:metabolism; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry*
chemical_list: D009282:Naphthalenesulfonates; D011994:Recombinant Proteins; C081786:cyclophilin B; C009497:2-(4-toluidino)-6-naphthalenesulfonic acid; D014364:Tryptophan; D021983:Cyclophilins; D019696:Peptidylprolyl Isomerase