scholarly journals Selecting highly structure-specific antibodies using structured synthetic mimics of the cystine knot protein sclerostin

2012 ◽  
Vol 25 (5) ◽  
pp. 251-259 ◽  
Author(s):  
J. W. Back ◽  
C. Frisch ◽  
K. Van Pee ◽  
V. Boschert ◽  
R. van Vught ◽  
...  
Keyword(s):  
Specific Antibodies ◽  
Cystine Knot ◽  
Cystine Knot Protein

High level expression of the Drosophila Toll receptor ectodomain and crystallization of its complex with the morphogen Spätzle

2013 ◽  
Vol 394 (8) ◽  
pp. 1091-1096 ◽  
Author(s):  
Marco Stelter ◽  
Uwe Fandrich ◽  
Kati Franzke ◽  
Angelika Schierhorn ◽  
Constanze Breithaupt ◽  
...  
Keyword(s):  
Immune Response ◽  
High Level Expression ◽  
Receptor Ligand ◽  
High Affinity ◽  
Cystine Knot ◽  
Toll Receptor ◽  
Cystine Knot Protein ◽  
High Yields ◽  
High Level ◽  
Affinity Interaction

Abstract Drosophila Toll receptors are involved in embryonic development and in the immune response of adult flies. In both processes, the Toll receptor ligand is the NGF-like cystine knot protein Spätzle. Here we present the expression of Toll receptor ectodomain in Schneider cells at high yields and demonstrate a high affinity interaction with the refolded and trypsin-processed Spätzle cystine knot domain dimer. Poorly and anisotropically diffracting crystals of the complex could be improved by deglycosylation and dehydration, paving the way for structural analyses of the Toll-Spätzle interaction.

Structural basis of BMP signalling inhibition by the cystine knot protein Noggin

Nature ◽  
2002 ◽  
Vol 420 (6916) ◽  
pp. 636-642 ◽  
Author(s):  
Jay Groppe ◽  
Jason Greenwald ◽  
Ezra Wiater ◽  
Joaquin Rodriguez-Leon ◽  
Aris N. Economides ◽  
...  
Keyword(s):  
Structural Basis ◽  
Cystine Knot ◽  
Cystine Knot Protein ◽  
Bmp Signalling

The race-specific elicitor AVR9 of the tomato pathogen Cladosporium fulvum : a cystine knot protein

FEBS Letters ◽  
1997 ◽  
Vol 404 (2-3) ◽  
pp. 153-158 ◽  
Author(s):  
Jacques Vervoort ◽  
Henno W van den Hooven ◽  
Axel Berg ◽  
Paul Vossen ◽  
Ralph Vogelsang ◽  
...  
Keyword(s):  
Cladosporium Fulvum ◽  
Cystine Knot ◽  
Cystine Knot Protein ◽  
Tomato Pathogen

scholarly journals The Structure of a Two-Disulfide Intermediate Assists in Elucidating the Oxidative Folding Pathway of a Cyclic Cystine Knot Protein

Structure ◽  
2008 ◽  
Vol 16 (6) ◽  
pp. 842-851 ◽  
Author(s):  
Maša Cemazar ◽  
Ajinkya Joshi ◽  
Norelle L. Daly ◽  
Alan E. Mark ◽  
David J. Craik
Keyword(s):  
Folding Pathway ◽  
Oxidative Folding ◽  
Cystine Knot ◽  
Cystine Knot Protein

STRUCTURAL BASIS OF BMP SIGNALING INHIBITION BY NOGGIN, A NOVEL TWELVE-MEMBERED CYSTINE KNOT PROTEIN

2003 ◽  
Vol 85 ◽  
pp. 52-58 ◽  
Author(s):  
JAY GROPPE ◽  
JASON GREENWALD ◽  
EZRA WIATER ◽  
JOAQUIN RODRIGUEZ-LEON ◽  
ARIS N. ECONOMIDES ◽  
...  
Keyword(s):  
Bmp Signaling ◽  
Structural Basis ◽  
Cystine Knot ◽  
Cystine Knot Protein

scholarly journals Biophysical Characterization of RefoldedDrosophilaSpätzle, a Cystine Knot Protein, Reveals Distinct Properties of Three Isoforms

2008 ◽  
Vol 283 (47) ◽  
pp. 32598-32609 ◽  
Author(s):  
Anita Hoffmann ◽  
Andreas Funkner ◽  
Piotr Neumann ◽  
Susanne Juhnke ◽  
Matthias Walther ◽  
...  
Keyword(s):  
Biophysical Characterization ◽  
Cystine Knot ◽  
Cystine Knot Protein

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

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