Complexation of tin(II) chloride by a novel macrocycle containing rhodium and nitrogen binding sites. The preparation and x-ray crystal structure of Rh2Sn2(CO)2Cl6[.mu.-2,6-bis(diphenylphosphino)pyridine]2

1985 ◽  
Vol 107 (24) ◽  
pp. 6936-6941 ◽  
Author(s):  
Alan L. Balch ◽  
Hakon Hope ◽  
Fred E. Wood
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
X Ray

Redox-responsive molybdenum mononitrosyl complexes incorporating cyclic polyether cation binding sites and x-ray crystal structure of [Mo(NO){HB(3,5-Me2C3N2H)3}{OCH2(CH2OCH2)3CH2O}]

1992 ◽  
Vol 31 (2) ◽  
pp. 263-267 ◽  
Author(s):  
Najat J. AlObaidi ◽  
Sithy S. Salam ◽  
Paul D. Beer ◽  
Christopher D. Bush ◽  
Thomas A. Hamor ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Cation Binding ◽  
X Ray ◽  
Redox Responsive

scholarly journals Self-association of an indole based guanidinium-carboxylate-zwitterion: formation of stable dimers in solution and the solid state

2010 ◽  
Vol 6 ◽  
Author(s):  
Carolin Rether ◽  
Wilhelm Sicking ◽  
Roland Boese ◽  
Carsten Schmuck
Keyword(s):  
Crystal Structure ◽  
Solid State ◽  
Binding Sites ◽  
Ion Pairs ◽  
Ph Titration ◽  
X Ray ◽  
Ideal Orientation ◽  
Guanidinium Group ◽  
Self Association ◽  
Zwitterion Formation

The indole based zwitterion 2 forms stable dimers held together by H-bond assisted ion pairs. Dimerisation was confirmed in the solid state and studied in solution using dilution NMR experiments. Even though zwitterion 2 forms very stable dimers even in DMSO, their stability is lower than of an analogous pyrrole based zwitterion 1. As revealed by the X-ray crystal structure the two binding sites in 2 cannot be planar due to steric interactions between the guanidinium group and a neighbouring aromatic CH. Hence the guanidinium moiety is twisted out of planarity from the rest of the molecule forcing the two monomers in dimer 2·2 to interact in a non-ideal orientation. Furthermore, the acidity of the NHs is lower than in 1 (as determined by UV-pH-titration) also leading to less efficient binding interactions.

Binding sites between palladium(II) and nucleosides or nucleotides and crystal structure of [Pd(diethylenetriamine)(guanosine)](ClO4)2

1980 ◽  
Vol 58 (4) ◽  
pp. 381-386 ◽  
Author(s):  
F. D. Rochon ◽  
P. C. Kong ◽  
B. Coulombe ◽  
R. Melanson
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Palladium Atom ◽  
X Ray Diffraction ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
R Factor ◽  
Square Planar ◽  
Purine Ring ◽  
Coordination Plane

The interactions between [Pd(dien)Cl]Cl and some nucleosides and nucleotides were studied by nmr. The binding site of guanosine, guanosinemonophosphoric acid, xanthosine, and inosine is N(7). Cytidine is coordinated to palladium through N(3). Adenosinemonophosphate acts as a bidentate, binding two different palladium atoms at N(1) and N(7).The crystal structure of [Pd(dien)(guanosine)](ClO4)2 has been determined by X-ray diffraction. The crystals are orthorhombic, space group P212121, with a = 13.422, b = 14.587, c = 12.432, and Z = 4. The structure was refined by block-diagonal least-squares analysis to a conventional R factor of 0.047 and a weighted Rw = 0.043. The coordination around the palladium atom is square planar. Guanosine is bonded to palladium through N(7). The planar purine ring makes an angle of 63.4° with the palladium coordination plane. The structure is stabilized by hydrogen bonding.

Supramolecular Complex Formed by Fumaric Acid and Piperazine: Crystal Structure, and Synthon Cooperation

2015 ◽  
Vol 1120-1121 ◽  
pp. 168-173
Author(s):  
Shi Ying Wang ◽  
Pei Qi Xing ◽  
Xiu Juan Geng ◽  
Rui Xin Chen
Keyword(s):  
Crystal Structure ◽  
Thermal Stability ◽  
Fumaric Acid ◽  
Binding Sites ◽  
Supramolecular Complex ◽  
X Ray Diffraction ◽  
X Ray ◽  
Hydrogen Bond Interactions ◽  
Supramolecular Chains ◽  
Thermal Stability Of

A new molecular complex constructed by fumaric acid with piperazine has been prepared and characterized by single crystal X-ray diffraction. The number of fumaric acid involved in the complex equals to the number of N-protonated binding sites in the piperazine molecule. The structure contained infinite 1D supramolecular chains held together by robust, primary O–H•••O charge-assisted hydrogen bonds, and the 2D sheet like pattern constructed via the expected carboxyl-piperazine heterosynthon. Persistent N–H•••O interactions were found to play an important role in the formation of the final 3D arrays. The five dominant supramolecular synthons in the crystal structure are the heteromeric carboxylic acid•••piperazine hydrogen bond interactions, which prevail in the presence of widely differing chemical functionalities. Thermal stability of the compound has been investigated by thermogravimetric analysis (TGA) of mass loss.

Probing the druggability of protein–protein interactions: targeting the Notch1 receptor ankyrin domain using a fragment-based approach

2011 ◽  
Vol 39 (5) ◽  
pp. 1327-1333 ◽  
Author(s):  
Noha Abdel-Rahman ◽  
Alfonso Martinez-Arias ◽  
Tom L. Blundell
Keyword(s):  
Crystal Structure ◽  
Protein Interactions ◽  
Binding Sites ◽  
Ternary Complex ◽  
Protein Protein Interactions ◽  
X Ray ◽  
Regulatory Systems ◽  
Protein Interfaces ◽  
Druggable Genome ◽  
Notch1 Receptor

In order to achieve greater selectivity in drug discovery, researchers in both academia and industry are targeting cell regulatory systems. This often involves targeting the protein–protein interactions of regulatory multiprotein assemblies. Protein–protein interfaces are widely recognized to be challenging targets as they tend to be large and relatively flat, and therefore usually do not have the concave binding sites that characterize the so-called ‘druggable genome’. One such prototypic multiprotein target is the Notch transcription complex, where an extensive network of protein–protein interactions stabilize the ternary complex comprising the ankyrin domain, CSL (CBF1/suppressor of Hairless/Lag-1) and MAML (Mastermind-like). Enhanced Notch activity is implicated in the development of T-ALL (T-cell acute lymphoblastic leukaemia) and selective inhibitors of Notch would be useful cancer medicines. In the present paper, we describe a fragment-based approach to explore the druggability of the ankyrin domain. Using biophysical methods and X-ray crystal structure analyses, we demonstrate that molecules can bind to the surface of the ankyrin domain at the interface region with CSL and MAML. We show that they probably represent starting points for designing larger compounds that can inhibit important protein–protein interactions that stabilize the Notch complex. Given the relatively featureless topography of the ankyrin domain, this unexpected development should encourage others to explore the druggability of such challenging multiprotein systems using fragment-based approaches.

scholarly journals X-ray Crystal Structure and Characterization of Halide-binding Sites of Human Myeloperoxidase at 1.8 Å Resolution

2000 ◽  
Vol 275 (16) ◽  
pp. 11964-11971 ◽  
Author(s):  
Tristan J. Fiedler ◽  
Curt A. Davey ◽  
Roger E. Fenna
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
X Ray

Notch ligand delta-like1: X-ray crystal structure and binding affinity

2015 ◽  
Vol 468 (1) ◽  
pp. 159-166 ◽  
Author(s):  
Nadia J. Kershaw ◽  
Nicole L. Church ◽  
Michael D.W. Griffin ◽  
Cindy S. Luo ◽  
Timothy E. Adams ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Affinity ◽  
Receptor Binding ◽  
Binding Sites ◽  
Notch Ligand ◽  
X Ray ◽  
Ligand Structure ◽  
Similarities And Differences

This X-ray crystal structure of the ectodomain of delta-like ligand-1 (Dll-1) represents the largest fragment of any Notch ligand structure to date. Comparison with the Jagged1 structures reveals similarities and differences between the ligand families and potential receptor binding sites.

A study on α-RuCl3 crystal structure by scanning tunneling microscopy

1989 ◽  
Vol 47 ◽  
pp. 30-31
Author(s):  
H.-J. Cantow ◽  
H. Hillebrecht ◽  
S. Magonov ◽  
H. W. Rotter ◽  
G. Thiele
Keyword(s):  
Crystal Structure ◽  
Density Distribution ◽  
Scanning Tunneling Microscopy ◽  
Electron Density ◽  
Structure Determination ◽  
Electron Density Distribution ◽  
Scanning Tunneling ◽  
Monoclinic Space Group ◽  
Tunneling Microscopy ◽  
X Ray

From X-ray analysis, the conclusions are drawn from averaged molecular informations. Thus, limitations are caused when analyzing systems whose symmetry is reduced due to interatomic interactions. In contrast, scanning tunneling microscopy (STM) directly images atomic scale surface electron density distribution, with a resolution up to fractions of Angstrom units. The crucial point is the correlation between the electron density distribution and the localization of individual atoms, which is reasonable in many cases. Thus, the use of STM images for crystal structure determination may be permitted. We tried to apply RuCl3 - a layered material with semiconductive properties - for such STM studies. From the X-ray analysis it has been assumed that α-form of this compound crystallizes in the monoclinic space group C2/m (AICI3 type). The chlorine atoms form an almost undistorted cubic closed package while Ru occupies 2/3 of the octahedral holes in every second layer building up a plane hexagon net (graphite net). Idealizing the arrangement of the chlorines a hexagonal symmetry would be expected. X-ray structure determination of isotypic compounds e.g. IrBr3 leads only to averaged positions of the metal atoms as there exist extended stacking faults of the metal layers.

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