ef hands การใช้

• The protein parvalbumin has EF hand motifs used for calcium binding.
• The Dockerin domain has two in-tandem repeats of a non-EF hand calcium binding motif.
• Calmodulin belongs to one of the two main groups of calcium-binding proteins, called EF hand proteins.
• Notably, the protein contains three EF hand motifs that function as binding sites for Ca 2 + ions.
• It contains a Ras exchange motif, a diacylglycerol-binding domain, and two calcium-binding EF hands.
• For example, calcium ions bind to the EF hand domains of calmodulin, allowing it to bind and activate calmodulin-dependent kinase.
• All scramblases contain an EF hand-like Ca 2 + binding domain that is probably responsible for the calcium activation of the enzyme.
• NCS-1 is a member of the neuronal calcium sensor family, a class of EF hand containing calcium-myristoyl-switch proteins.
• IBA1 is a 17-kDa EF hand protein that is specifically expressed in macrophages / microglia and is upregulated during the activation of these cells.
• However, only three of these EF hands are functional in NCS-1 ( the most N-terminal EF hand does not bind calcium ).
• However, only three of these EF hands are functional in NCS-1 ( the most N-terminal EF hand does not bind calcium ).
• Upon activation of the IP3 receptor, the calcium concentration in the endoplasmic reticulum decreases, which is sensed by STIM1, via its EF hand domain.
• EF hands are structural helix-loop-helix protein subunits that have a high affinity for calcium ions, and a moderate affinity for magnesium ions.
• The anaerobic bacterial dockerins are homologous to EF hands ( calcium-binding motifs ) and require calcium for activity whereas the fungal dockerin does not require calcium.
• Upon binding calcium, helix 3 of S100A1 re-orients from being relatively antiparallel to C-terminal helix and the linker connecting the two EF hand domains.
• The WW domain is the primary site of interaction between dystrophin or utrophin and dystroglycan, while the EF hand and ZZ-type zinc finger domains stabilise and strengthen this interaction.
• PLC-?1 also possesses a classical leucine-rich nuclear export signal ( NES ) in its EF hand motif, as well as a Nuclear localization signal within its linker region.
• It has three EF hand motifs and is structurally related to calmodulin and troponin C . Parvalbumin is localised in fast-contracting muscles, where its levels are highest, as well as in the brain and some endocrine tissues.
• The Ca 2 +-binding site is a novel EF hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca 2 + binding and regulation in the intact myosin molecule.
• It binds to BMP-4 and TGF-?1, but not Activin A . It contains an FS module ( a follistatin-like sequence containing 10 conserved cysteine residues ), a Kazal-type serine protease inhibitor domain, 2 EF hand domains, and a Von Willebrand factor type C domain.