Ferri S

References (2)

Title : Binding profile of benextramine at neuropeptide Y receptor subtypes in rat brain areas - Melchiorre_1994_Eur.J.Pharmacol_265_93
Author(s) : Melchiorre C , Romualdi P , Bolognesi ML , Donatini A , Ferri S
Ref : European Journal of Pharmacology , 265 :93 , 1994
Abstract : Binding studies in rat whole brain, frontoparietal cortex and brainstem membrane preparations revealed that benextramine displaced [3H]neuropeptide Y specific binding from a low and a high affinity site with IC50 values in the microM (36 +/- 2, 4.4 +/- 1.4 and 300 +/- 120 microM, respectively) and the pM (29.3 +/- 12.1, 0.35 +/- 0.11 and 0.42 +/- 0.03 pM, respectively) range, whereas in rat hippocampus benextramine displaced [3H]neuropeptide Y specific binding from one site only with an IC50 value of 22.8 +/- 5.7 microM. With the exception of frontoparietal cortex binding assay, benextramine was not able to completely inhibit [3H]neuropeptide Y specific binding revealing the presence of a benextramine nonsensitive third binding site. Benextramine pretreatment followed by membrane washing demonstrated that benextramine inhibited irreversibly both high and low affinity sites.
ESTHER : Melchiorre_1994_Eur.J.Pharmacol_265_93
PubMedSearch : Melchiorre_1994_Eur.J.Pharmacol_265_93
PubMedID: 7883034

Title : Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi - Lawson_1994_Biochemistry_33_9382
Author(s) : Lawson DM , Derewenda U , Serre L , Ferri S , Szittner R , Wei Y , Meighen EA , Derewenda ZS
Ref : Biochemistry , 33 :9382 , 1994
Abstract : The crystal structure of a myristoyl acyl carrier protein specific thioesterase (C14ACP-TE) from a bioluminescent bacterium, Vibrio harveyi, was solved by multiple isomorphous replacement methods and refined to an R factor of 22% at 2.1-A resolution. This is the first elucidation of a three-dimensional structure of a thioesterase. The overall tertiary architecture of the enzyme resembles closely the consensus fold of the rapidly expanding superfamily of alpha/beta hydrolases, although there is no detectable homology with any of its members at the amino acid sequence level. Particularly striking similarity exists between the C14ACP-TE structure and that of haloalkane dehalogenase from Xanthobacter autotrophicus. Contrary to the conclusions of earlier studies [Ferri, S. R., & Meighen, E. A. (1991) J. Biol. Chem. 266, 12852-12857] which implicated Ser77 in catalysis, the crystal structure of C14ACP-TE reveals a lipase-like catalytic triad made up of Ser114, His241, and Asp211. Surprisingly, the gamma-turn with Ser114 in a strained secondary conformation (phi = 53 degrees, psi = -127 degrees), characteristic of the so-called nucleophilic elbow, does not conform to the frequently invoked lipase/esterase consensus sequence (Gly-X-Ser-X-Gly), as the positions of both glycines are occupied by larger amino acids. Site-directed mutagenesis and radioactive labeling support the catalytic function of Ser114. Crystallographic analysis of the Ser77-->Gly mutant at 2.5-A resolution revealed no structural changes; in both cases the loop containing the residue in position 77 is disordered.
ESTHER : Lawson_1994_Biochemistry_33_9382
PubMedSearch : Lawson_1994_Biochemistry_33_9382
PubMedID: 8068614
Gene_locus related to this paper: pholu-lxd1 , phopo-luxd , vibha-1luxd