Ligand-Free Suzuki–Miyaura Coupling with Sulfur-Modified Gold-Supported Palladium in the Synthesis of a Conformationally-Restricted Cyclopropane Compound Library with Three-Dimensional Diversity

2014 ◽  
Vol 16 (5) ◽  
pp. 215-220 ◽  
Author(s):  
Mitsuhiro Arisawa ◽  
Takatoshi Sato ◽  
Naoyuki Hoshiya ◽  
Mohammad Al-Amin ◽  
Yuji Kogami ◽  
...  
2012 ◽  
Vol 53 (52) ◽  
pp. 7044-7051 ◽  
Author(s):  
Dharminder Sharma ◽  
Sandeep Kumar ◽  
Arun K. Shil ◽  
Nitul Ranjan Guha ◽  
Bandna ◽  
...  

2008 ◽  
Vol 350 (13) ◽  
pp. 1968-1974 ◽  
Author(s):  
Pravin R. Likhar ◽  
Moumita Roy ◽  
Sarabindu Roy ◽  
M. S. Subhas ◽  
M. Lakshmi Kantam ◽  
...  

2005 ◽  
Vol 168 (7) ◽  
pp. 1109-1118 ◽  
Author(s):  
Brian D. Adair ◽  
Jian-Ping Xiong ◽  
Catherine Maddock ◽  
Simon L. Goodman ◽  
M. Amin Arnaout ◽  
...  

Integrins are αβ heterodimeric cell surface receptors that mediate transmembrane signaling by binding extracellular and cytoplasmic ligands. The ectodomain of integrin αVβ3 crystallizes in a bent, genuflexed conformation considered to be inactive (unable to bind physiological ligands in solution) unless it is fully extended by activating stimuli. We generated a stable, soluble complex of the Mn2+-bound αVβ3 ectodomain with a fragment of fibronectin (FN) containing type III domains 7 to 10 and the EDB domain (FN7-EDB-10). Transmission electron microscopy and single particle image analysis were used to determine the three-dimensional structure of this complex. Most αVβ3 particles, whether unliganded or FN-bound, displayed compact, triangular shapes. A difference map comparing ligand-free and FN-bound αVβ3 revealed density that could accommodate the RGD-containing FN10 in proximity to the ligand-binding site of β3, with FN9 just adjacent to the synergy site binding region of αV. We conclude that the ectodomain of αVβ3 manifests a bent conformation that is capable of stably binding a physiological ligand in solution.


ChemInform ◽  
2012 ◽  
Vol 43 (52) ◽  
pp. no-no
Author(s):  
Bandna Bandna ◽  
Nitul Ranjan Guha ◽  
Arun K. Shil ◽  
Dharminder Sharma ◽  
Pralay Das

1995 ◽  
Vol 348 (1323) ◽  
pp. 113-119 ◽  

The three-dimensional structure of the E. coli chaperonin, GroEL, has been determined crystallo-graphically and refined to 2.7 Å in two crystal forms: an orthorhombic form from high salt and a monoclinic form from polyethylene glycol. The former is ligand free, the latter is both liganded with ATP analogues and ligand free. These structures provide a structural scaffold upon which to interpret extensive mutagenesis and biochemical studies. GroEL contains two sevenfold rotationally symmetric rings of identical 547-amino acid subunits. The rings are arranged ‘back-to-back’ with exact dyad symmetry to form a stubby cylinder that is 146 Å high with an outer diameter of about 143 Å. The cylinder has a substantial central channel that is unobstructed for the entire length of the cylinder and has a diameter of about 45 Å except for large bulges that lead into a sevenfold symmetric array of elliptical side windows in each ring. Each subunit is composed of three distinct domains: (i) an ‘equatorial’ domain that contains the N- and C-terminus and the ATP-binding pocket, .(ii) an ‘apical domain’ that forms the opening of the central channel and contains poorly ordered segments that mutational studies implicate in binding unfolded polypeptides and GroES, and (iii) an intermediate domain tht connects the other two domains and may serve to transmit allosteric adjustments.


2011 ◽  
Vol 50 (12) ◽  
pp. 5841-5847 ◽  
Author(s):  
Yunxin Liu ◽  
Dingsheng Wang ◽  
Qing Peng ◽  
Deren Chu ◽  
Xiangwen Liu ◽  
...  

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