Vasoinhibin comprises a three-helix bundle and its antiangiogenic domain is located within the first 79 residues
نویسندگان
چکیده
منابع مشابه
Conduction disturbances located within the His bundle.
SUMMARY Four patients are described with different degrees of conduction disturbance within the His bundle. In one patient with a Mobitz type II atrioventricular (A-V) block with normal QRS complexes the blocked atrial beats were followed by a His potential. Since the QRS complexes of the conducted beats were completely normal, the site of the block was thought to be in the distal part of the H...
متن کاملExtension of a three-helix bundle domain of myosin VI and key role of calmodulins.
The molecular motor protein myosin VI moves toward the minus-end of actin filaments with a step size of 30-36 nm. Such large step size either drastically limits the degree of complex formation between dimer subunits to leave enough length for the lever arms, or requires an extension of the lever arms' crystallographically observed structure. Recent experimental work proposed that myosin VI dime...
متن کاملThree-helix-bundle protein in a Ramachandran model.
We study the thermodynamic behavior of a model protein with 54 amino acids that forms a three-helix bundle in its native state. The model contains three types of amino acids and five to six atoms per amino acid and has the Ramachandran torsional angles phi(i), psi(i) as its degrees of freedom. The force field is based on hydrogen bonds and effective hydrophobicity forces. For a suitable choice ...
متن کاملFolding thermodynamics of a model three-helix-bundle protein.
The calculated folding thermodynamics of a simple off-lattice three-helix-bundle protein model under equilibrium conditions shows the experimentally observed protein transitions: a collapse transition, a disordered-to-ordered globule transition, a globule to native-state transition, and the transition from the active native state to a frozen inactive state. The cooperativity and physical origin...
متن کاملGTP-dependent packing of a three-helix bundle is required for atlastin-mediated fusion.
The mechanisms governing atlastin-mediated membrane fusion are unknown. Here we demonstrate that a three-helix bundle (3HB) within the middle domain is required for oligomerization. Mutation of core hydrophobic residues within these helices inactivates atlastin function by preventing membrane tethering and the subsequent fusion. GTP binding induces a conformational change that reorients the GTP...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Scientific Reports
سال: 2018
ISSN: 2045-2322
DOI: 10.1038/s41598-018-35383-7