Structural Insight into Integrin Recognition and Anticancer Activity of Echistatin.

Echistatin (Ech) is a short disintegrin with a long NPHKGPAT C-terminal tail. We determined the 3-D structure of Ech by X-ray crystallography. Superimposition of the structures of chains A and B showed conformational differences in their RGD loops and C-termini.

Effects of the RGD loop and C-terminus of rhodostomin on regulating integrin αIIbβ3 recognition.

Rhodostomin (Rho) is a medium disintegrin containing a 48PRGDMP motif. We here showed that Rho proteins with P48A, M52W, and P53N mutations can selectively inhibit integrin αIIbβ3. To study the roles of the RGD loop and C-terminal region in disintegrins, we expressed Rho 48PRGDMP and 48ARGDWN mutants in Pichia pastoris containing 65P, 65PR, 65PRYH, 65PRNGLYG, and 65PRNPWNG C-terminal sequences.

Finger evolution of a gas bubble driven by atmospheric pressure plasma.

We report the generation and evolution of a finger-shaped bubble in liquid by dielectric discharge setup. The spherical gas bubble is deformed into a finger-shaped bubble after the ignition of plasma. The presence of the filamentary discharge in the bubble not only provides the local heating to the bubble, it also changes the distribution of the electric field in the bubble and the bubble mutually provides the pathway to the discharge.

Dynamics and functional differences between dendroaspin and rhodostomin: insights into protein scaffolds in integrin recognition.

Dendroaspin (Den) and rhodostomin (Rho) are snake venom proteins containing a PRGDMP motif. Although Den and Rho have different 3D structures, they are highly potent integrin inhibitors. To study their structure, function, and dynamics relationships, we expressed Den and Rho in Pichia pastoris.

Expression in Pichia pastoris and characterization of echistatin, an RGD-containing short disintegrin.

Echistatin (Ech) is a potent inhibitor of integrins and was isolated from snake Echis carinatus. To facilitate the study on the molecular determinants of integrin-ligand interactions, we expressed recombinant Ech and its mutants in the Pichia pastoris (P. pastoris) expression system and purified them to homogeneity with the yields of 2-7 mg/L.

Effect of P to A mutation of the N-terminal residue adjacent to the Rgd motif on rhodostomin: importance of dynamics in integrin recognition.

Rhodostomin (Rho) is an RGD protein that specifically inhibits integrins. We found that Rho mutants with the P48A mutation 4.4-11.

Solution structure and backbone dynamics of the DNA-binding domain of FOXP1: insight into its domain swapping and DNA binding.

FOXP1 belongs to the P-subfamily of forkhead transcription factors and contains a conserved forkhead DNA-binding domain. According to size exclusion chromatography analysis, the forkhead domain of FOXP1 existed as a mixture of monomer and dimer. The dissociation constants of the forkhead domain of wild-type, C61S, and C61Y mutants of FOXP1 were 27.

Effect of D to E mutation of the RGD motif in rhodostomin on its activity, structure, and dynamics: importance of the interactions between the D residue and integrin.

Rhodostomin (Rho) is a snake venom protein containing an RGD motif that specifically inhibits the integrin-binding function. Rho produced in Pichia pastoris inhibits platelet aggregation with a K(I) of 78 nM as potent as native Rho. In contrast, its D51E mutant inhibits platelet aggregation with a K(I) of 49 muM.

Solution structure of gamma-bungarotoxin: the functional significance of amino acid residues flanking the RGD motif in integrin binding.

Gamma-bungarotoxin, a snake venom protein isolated from Bungarus multicinctus, contains 68 amino acids, including 10 cysteine residues and a TAVRGDGP sequence at positions 30-37. The solution structure of gamma-bungarotoxin has been determined by nuclear magnetic resonance (NMR) spectroscopy. The structure is similar to that of the short-chain neurotoxins that contain three loops extending from a disulfide-bridged core.