High-resolution three-dimensional structure of a single zinc finger from a human enhancer binding protein in solution

Biochemistry ◽  
1990 ◽  
Vol 29 (40) ◽  
pp. 9324-9334 ◽  
Author(s):  
James G. Omichinski ◽  
G. Marius Clore ◽  
Ettore Appella ◽  
Kazuyasu Sakaguchi ◽  
Angela M. Gronenborn
Keyword(s):  
High Resolution ◽  
Zinc Finger ◽  
Binding Protein ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Enhancer Binding Protein

scholarly journals Three-dimensional structure of actin filaments and of an actin gel made with actin-binding protein.

1983 ◽  
Vol 96 (5) ◽  
pp. 1400-1413 ◽  
Author(s):  
R Niederman ◽  
P C Amrein ◽  
J Hartwig
Keyword(s):  
Actin Filaments ◽  
Binding Protein ◽  
Three Dimensional ◽  
Actin Binding ◽  
Dimensional Structure ◽  
Molar Ratio ◽  
Computer Assisted ◽  
Three Dimensional Structure ◽  
Actin Binding Protein ◽  
Critical Point Drying

Purified muscle actin and mixtures of actin and actin-binding protein were examined in the transmission electron microscope after fixation, critical point drying, and rotary shadowing. The three-dimensional structure of the protein assemblies was analyzed by a computer-assisted graphic analysis applicable to generalized filament networks. This analysis yielded information concerning the frequency of filament intersections, the filament length between these intersections, the angle at which filaments branch at these intersections, and the concentration of filaments within a defined volume. Purified actin at a concentration of 1 mg/ml assembled into a uniform mass of long filaments which overlap at random angles between 0 degrees and 90 degrees. Actin in the presence of macrophage actin-binding protein assembled into short, straight filaments, organized in a perpendicular branching network. The distance between branch points was inversely related to the molar ratio of actin-binding protein to actin. This distance was what would be predicted if actin filaments grew at right angles off of nucleation sites on the two ends of actin-binding protein dimers, and then annealed. The results suggest that actin in combination with actin-binding protein self-assembles to form a three-dimensional network resembling the peripheral cytoskeleton of motile cells.

scholarly journals Three-dimensional structure of fatty-acid-binding protein from bovine heart

1991 ◽  
Vol 199 (2) ◽  
pp. 271-276 ◽  
Author(s):  
Anke MULLER-FAHRNOW ◽  
Ursula EGNER ◽  
T. Alwyn JONES ◽  
Heinz RUDEL ◽  
Friedrich SPENER ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Fatty Acid Binding ◽  
Three Dimensional Structure ◽  
Acid Binding Protein ◽  
Bovine Heart

scholarly journals Advances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, a Model of G-Protein-Coupled Receptors (GPCRs)†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (26) ◽  
pp. 7761-7772 ◽  
Author(s):  
David C. Teller ◽  
Tetsuji Okada ◽  
Craig A. Behnke ◽  
Krzysztof Palczewski ◽  
Ronald E. Stenkamp
Keyword(s):  
High Resolution ◽  
G Protein ◽  
Three Dimensional ◽  
G Protein Coupled Receptors ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
G Protein Coupled

High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1

Biochemistry ◽  
1992 ◽  
Vol 31 (16) ◽  
pp. 3907-3917 ◽  
Author(s):  
James G. Omichinski ◽  
G. Marius Clore ◽  
Mark Robien ◽  
Kazuyasu Sakaguchi ◽  
Ettore Appella ◽  
...  
Keyword(s):  
High Resolution ◽  
Zinc Finger ◽  
Solution Structure ◽  
Binding Protein ◽  
Enhancer Binding Protein
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