Coiled-coiled domains as a mechanism to stop haemorrhage after renal biopsies
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چکیده
منابع مشابه
Coiled-Coil Domains of SUN Proteins as Intrinsic Dynamic Regulators.
SUN proteins are the core components of LINC complexes that span across the nuclear envelope for nuclear positioning and migration. SUN proteins contain at least one predicted coiled-coil domain preceding the SUN domain. Here, we found that the two coiled-coil domains (CC1 and CC2) of SUN2 exhibit distinct oligomeric states. CC2 is a monomer in solution. The structure of the CC2-SUN monomer rev...
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Spectrin repeats have been largely considered as passive linkers or spacers with little functional role other than to convey flexibility to a protein. Whilst this is undoubtedly part of their function, it is by no means all. Whilst the overt structure of all spectrin repeats is a simple triple-helical coiled coil, the linkages between repeats and the surface properties of repeats vary widely. S...
متن کاملCoiled coils and SAH domains in cytoskeletal molecular motors.
Cytoskeletal motors include myosins, kinesins and dyneins. Myosins move along tracks of actin filaments, whereas kinesins and dyneins move along microtubules. Many of these motors are involved in trafficking cargo in cells. However, myosins are mostly monomeric, whereas kinesins are mostly dimeric, owing to the presence of a coiled coil. Some myosins (myosins 6, 7 and 10) contain an SAH (single...
متن کاملStabilization of coiled-coil peptide domains by introduction of trifluoroleucine.
Substitution of leucine residues by 5,5,5-trifluoroleucine at the d-positions of the leucine zipper peptide GCN4-p1d increases the thermal stability of the coiled-coil structure. The midpoint thermal unfolding temperature of the fluorinated peptide is elevated by 13 degrees C at 30 microM peptide concentration. The modified peptide is more resistant to chaotropic denaturants, and the free energ...
متن کاملCoiled coil domains: stability, specificity, and biological implications.
The coiled coil is a common structural motif, formed by approximately 3 ± 5% of all amino acids in proteins. Typically, it consists of two to five -helices wrapped around each other into a left-handed helix to form a supercoil. Whereas regular -helices go through 3.6 residues for each complete turn of the helix, the distortion imposed upon each helix within a left-handed coiled coil lowers this...
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ژورنال
عنوان ژورنال: Nephrology Dialysis Transplantation
سال: 2008
ISSN: 0931-0509,1460-2385
DOI: 10.1093/ndt/gfn227