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  • repeats
  • actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). (nih.gov)
  • The crescent shape adopted by a series of leucine-rich repeats creates a solvent-exposed, elongated, concave surface of parallel β-strands that act as a scaffold for protein-protein interactions. (cellsignal.com)
  • affinity
  • domains bind with high affinity (low µM or nM Kd) to specific phosphoinositides such as phosphatidylinositol- 4,5-bisphosphate, PI-3, 4-P2 or PI-3,4,5-P3. (cellsignal.com)
  • bound
  • Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. (ebi.ac.uk)
  • The double TUDOR domain of JMJD2A bound to a tri-methylated histone H3-K4. (cellsignal.com)
  • Dystrophin
  • In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. (nih.gov)
  • alignment
  • Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. (nih.gov)
  • consists
  • It consists of a mineral core of hydrated ferric oxide, and a multi-subunit protein shell that encloses the former and assures its solubility in an aqueous environment. (ebi.ac.uk)
  • vesicular
  • The major components of the endosomal sorting complex required for transport (ESCRT) complex are proteins recruited at different stages of the vesicular transport pathway. (cellsignal.com)