Quantitative Evaluation of Each Catalytic Subsite of Cathepsin B for Inhibitory Activity Based on Inhibitory Activity–Binding Mode Relationship of Epoxysuccinyl Inhibitors by X-ray Crystal Structure Analyses of Complexes

2006 ◽  
Vol 362 (5) ◽  
pp. 979-993 ◽  
Author(s):  
Daiya Watanabe ◽  
Atsushi Yamamoto ◽  
Koji Tomoo ◽  
Keita Matsumoto ◽  
Mitsuo Murata ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Quantitative Evaluation ◽  
Inhibitory Activity ◽  
Cathepsin B ◽  
Binding Mode ◽  
X Ray ◽  
Relationship Of

scholarly journals Crystal structure and molecular docking studies of new pyrazole-4-carboxamides

2019 ◽  
Vol 25 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Li Qiao ◽  
Peng-Peng Cai ◽  
Zhong-Hua Shen ◽  
Hong-Ke Wu ◽  
Cheng-Xia Tan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Docking ◽  
Botrytis Cinerea ◽  
Inhibitory Activity ◽  
Docking Studies ◽  
Active Group ◽  
X Ray Diffraction ◽  
X Ray ◽  
Molecular Docking Studies ◽  
H Nmr

AbstractTwo pyrazol-4-carboxamides, 3-(difluoromethyl)-N-(mesitylcarbamoyl)-1-methyl-1H-pyrazole-4-carboxa-mide (7a) and 3-(difluoromethyl)-N-((3,5-dimethylphenyl) carbamoyl)-1-methyl-1H-pyrazole-4-carboxamide (7b) were synthesized and their structures were confirmed by the aid of 1H NMR and HRMS analyses. The structure of the pyrazole-4-carboxamide, 7a was also determined by X-ray diffraction. The preliminary activity results demonstrate that these two compounds exhibit good inhibitory activity against Botrytis cinerea. Further docking results indicated that the key active group is difluoromethyl pyrazole moiety.

Binding mode of thiocyanate in palladium(II) complexes: x-ray crystal structure of cis-(isothiocyanato)(thiocyanato)bis(1-phenyl-3,4-dimethylphosphole)palladium(II)

1982 ◽  
Vol 21 (3) ◽  
pp. 1200-1204 ◽  
Author(s):  
John H. Nelson ◽  
J. Jeffrey. MacDougall ◽  
Nathaniel W. Alcock ◽  
Francois. Mathey
Keyword(s):  
Crystal Structure ◽  
Binding Mode ◽  
X Ray

scholarly journals X-ray diffraction studies of enkephalins. Crystal structure of [(4′-bromo) Phe4,Leu5]enkephalin

1984 ◽  
Vol 218 (3) ◽  
pp. 677-689 ◽  
Author(s):  
T Ishida ◽  
M Kenmotsu ◽  
Y Mino ◽  
M Inoue ◽  
T Fujiwara ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Least Squares Method ◽  
Heavy Atom ◽  
Three Dimensional ◽  
Diffraction Method ◽  
Biologically Active ◽  
Type I ◽  
X Ray Diffraction ◽  
X Ray ◽  
Relationship Of

In order to investigate the structure-activity relationship of [Leu5]- and [Met5]enkephalins, [(4′-bromo)Phe4, Leu5]-, [(4′-bromo)Phe4, Met5]- and [Met5] enkephalins were synthesized and crystallized. The crystal structure of [(4′-bromo) Phe4, Leu5]- enkephalin was determined by X-ray diffraction method using the heavy atom method and refined to R = 0.092 by the least-squares method. The molecule in this crystal took essentially the same type I' beta-turn conformation found in [Leu5]enkephalin [Smith & Griffin (1978) Science 199, 1214-1216). On the other hand, the preliminary three-dimensional Patterson analyses showed that the most probable conformations of [(4′-bromo)Phe4,Met5]- and [Met5]enkephalins are both the dimeric extended forms. Based on these insights, the biologically active conformation of enkephalin was discussed in relation to the mu- and delta-receptors.

scholarly journals Crystal structure of human RIOK2 bound to a specific inhibitor

Open Biology ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 190037 ◽  
Author(s):  
Jing Wang ◽  
Thibault Varin ◽  
Michal Vieth ◽  
Jonathan M. Elkins
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Hydrophobic Interactions ◽  
Specific Inhibitor ◽  
Binding Mode ◽  
Atp Binding ◽  
Active Site Residues ◽  
Atp Binding Site ◽  
Universal Family ◽  
Relationship Of

The RIO kinases (RIOKs) are a universal family of atypical kinases that are essential for assembly of the pre-40S ribosome complex. Here, we present the crystal structure of human RIO kinase 2 (RIOK2) bound to a specific inhibitor. This first crystal structure of an inhibitor-bound RIO kinase reveals the binding mode of the inhibitor and explains the structure–activity relationship of the inhibitor series. The inhibitor binds in the ATP-binding site and forms extensive hydrophobic interactions with residues at the entrance to the ATP-binding site. Analysis of the conservation of active site residues reveals the reasons for the specificity of the inhibitor for RIOK2 over RIOK1 and RIOK3, and it provides a template for inhibitor design against the human RIOK family.

β-Ca11B2Si4O22: six-fold twinning, crystal structure and thermal expansion

2018 ◽  
Vol 233 (6) ◽  
pp. 379-390 ◽  
Author(s):  
Sergey N. Volkov ◽  
Valentina A. Yukhno ◽  
Rimma S. Bubnova ◽  
Vladimir V. Shilovskikh
Keyword(s):  
Crystal Structure ◽  
Thermal Expansion ◽  
High Temperature ◽  
Electron Backscatter Diffraction ◽  
Monoclinic Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Electron Backscatter ◽  
Backscatter Diffraction ◽  
Relationship Of

Abstract The low-temperature polymorph β-Ca11B2Si4O22 crystallizes as a monoclinic structure [space group is P21/c, a=14.059(9), b=6.834(5), c=10.597(7) Å, β=100.735(8)°]. The crystal investigated by single-crystal X-ray diffraction was a twin composed of six individuals. The crystal structure is similar to that of mineral spurrite, Ca5(SiO4)2CO3, and can be described as a framework of [CaO5] and [CaO6] polyhedra, the cavities of which are filled with [SiO4] and [BO3] groups. The orientation relationship of twin domains was investigated by electron backscatter diffraction (EBSD). Thermal expansion was studied by high-temperature X-ray powder diffraction. It is slightly anisotropic: α11=10, α22=16, α33=12×10−6°C−1 at 200°C.

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