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Oligomerization and Multimerization Are Critical for Angiopoietin-1 to Bind and Phosphorylate Tie2*
Proper oligomerization of Ang1 having at least four subunits by the intermolecular disulfide linkage involving cysteines 41 and 54 is critical for Tie2 binding and activation. Expand
Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer
The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined and it is shown that the right-handed coiled coil reveals large hydrophobic cavities that are filled with water molecules. Expand
COMP-Ang1: a designed angiopoietin-1 variant with nonleaky angiogenic activity.
  • C. Cho, R. Kammerer, +12 authors G. Koh
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 13 April 2004
By replacing the N-terminal portion of Ang1 with the short coiled-coil domain of cartilage oligomeric matrix protein (COMP), this variant is a soluble, stable, and potent Ang1 variant, COMP-Ang1, which is more potent than native Ang1 in phosphorylating the tyrosine kinase with Ig and epidermal growth factor homology domain 2 (Tie2) receptor and Akt in primary cultured endothelial cells. Expand
Cortexillins, Major Determinants of Cell Shape and Size, Are Actin-Bundling Proteins with a Parallel Coiled-Coil Tail
Cortexillins I and II of D. discoideum constitute a novel subfamily of proteins with actin-binding sites of the alpha-actinin/spectrin type that are enriched in the cortex of locomoting cells, primarily at the anterior and posterior ends. Expand
The Crystal Structure of a Five-Stranded Coiled Coil in COMP: A Prototype Ion Channel?
The crystal structure of a parallel pentameric coiled coil, constituting the oligomerization domain in the cartilage oligomeric matrix protein (COMP), was determined at 2.05 angstroms resolution and has marked similarities with proposed models of thepentameric transmembrane ion channels in phospholamban and the acetylcholine receptor. Expand
Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A
The high-resolution crystal structure of the BoNT/A receptor-binding domain (BoNT/ a-RBD) in complex with the SV2C luminal domain (SV2C-LD) is determined, providing a strong platform for the development of novel antitoxin agents and for the rational design of Bo NT/A variants with improved therapeutic properties. Expand
A conserved trimerization motif controls the topology of short coiled coils.
It is demonstrated that trimerization of short coiled coils is determined by a distinct structural motif that encompasses specific networks of surface salt bridges and optimal hydrophobic packing interactions, and may be of interest for viral drug development strategies. Expand
Subdomain-Specific Localization of Climp-63 (P63) in the Endoplasmic Reticulum Is Mediated by Its Luminal α-Helical Segment
It is shown that concentration of CLIMP-63 into patches may enhance microtubule binding on the cytosolic side and contribute to ER morphology by the formation of a protein scaffold in the lumen of the ER. Expand
Remorins form a novel family of coiled coil-forming oligomeric and filamentous proteins associated with apical, vascular and embryonic tissues in plants
Electron microscopy of purified preparations of four different recombinant remorins, one from potato, two divergent isologs from tomato, and one from Arabidopsis thaliana, demonstrated that the proteins form highly similar filamentous structures. Expand
Molecular basis of coiled-coil formation
This work identifies and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil, and demonstrates that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. Expand