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

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

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.

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

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

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

Organization of tight junctions in the choroid plexus epithelium

1978 ◽  
Vol 36 (2) ◽  
pp. 336-337
Author(s):  
B. Van Deurs ◽  
J. K. Koehler
Keyword(s):  
Choroid Plexus ◽  
Present Report ◽  
Freeze Fracture ◽  
Barrier Properties ◽  
Cell Junctions ◽  
Structural Basis ◽  
Apical Surface ◽  
Choroid Plexus Epithelium ◽  
Solid Nitrogen ◽  
Special Composition

The choroid plexus epithelium constitutes a blood-cerebrospinal fluid (CSF) barrier, and is involved in regulation of the special composition of the CSF. The epithelium is provided with an ouabain-sensitive Na/K-pump located at the apical surface, actively pumping ions into the CSF. The choroid plexus epithelium has been described as “leaky” with a low transepithelial resistance, and a passive transepithelial flux following a paracellular route (intercellular spaces and cell junctions) also takes place. The present report describes the structural basis for these “barrier” properties of the choroid plexus epithelium as revealed by freeze fracture.Choroid plexus from the lateral, third and fourth ventricles of rats were used. The tissue was fixed in glutaraldehyde and stored in 30% glycerol. Freezing was performed either in liquid nitrogen-cooled Freon 22, or directly in a mixture of liquid and solid nitrogen prepared in a special vacuum chamber. The latter method was always used, and considered necessary, when preparations of complementary (double) replicas were made.

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