• A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. (wikipedia.org)
  • Leucine zippers are a dimerization motif of the bZIP (Basic-region leucine zipper) class of eukaryotic transcription factors. (wikipedia.org)
  • The predicted protein encodes a leucine zipper motif. (nih.gov)
  • Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein. (umassmed.edu)
  • What is a leucine zipper motif? (neighborshateus.com)
  • How is the leucine zipper motif related to DNA binding? (neighborshateus.com)
  • The Leucine Zipper Motif Mediates Both DNA Binding and Protein Dimerization. (neighborshateus.com)
  • Here, we have investigated the importance of an unusual leucine zipper coiled-coil motif present in the C-terminal noncatalytic domain of the Nek2 kinase. (unibas.ch)
  • Recombinant Nek2 overexpressed in insect cells also formed a 6 S complex, whereas a Nek2 mutant specifically lacking the leucine zipper motif was monomeric. (unibas.ch)
  • Using yeast two-hybrid interaction analyses and coprecipitation assays, we found that Nek2 can indeed form homodimers both in vivo and in vitro and that this dimerization specifically required the leucine zipper motif. (unibas.ch)
  • Thus, this study reveals not only an important mechanism for the regulation of the Nek2 kinase but, furthermore, highlights an unusual organization of a leucine zipper dimerization motif. (unibas.ch)
  • We have detected a leucine zipper-like motif in the ectodomain of Sendal virus fusion protein (a. a. 269-307) which is extremely conserved in the family of Sendal viruses. (tau.ac.il)
  • In order to find out a possible role of this motif, a thirty nine residue peptide corresponding to this domain, designated SV-269, and a mutant peptide, MuSV-269, with a heptadic leucine and glutamic acid interchanged their positions, were synthesized and labeled with fluorescent probes at their N-terminal amino acids. (tau.ac.il)
  • The data suggest a possible rote of this putative leucine zipper motif in the assembly of the Sendal virus fusion protein in solution and membrane. (tau.ac.il)
  • Leucine zipper motifs are considered a subtype of coiled coils, which are built by two or more alpha helices that are wound around each other to form a supercoil. (wikipedia.org)
  • Owing to the stability of their coiled coil structure leucine zipper (LZ) domains of bZIP factors are widely employed as dimerization motifs in protein engineering studies. (neighborshateus.com)
  • Leucine zipper domains are made up of two motifs: a basic region that recognizes a specific DNA sequence and a series of leucines spaced 7 residues apart along an α-helix (leucine zipper) that mediate dimerization. (neighborshateus.com)
  • In addition, we have used yeast to investigate the role of the Myc helix-loop-helix (HLH) and leucine zipper (LZ) motifs in mediating Max-dependent DNA-binding and transcriptional activation in vivo using HLH/LZ mutants generated by site-directed mutagenesis. (ox.ac.uk)
  • The polypeptide segments containing these periodic arrays of leucine residues were proposed to exist in an alpha-helical conformation and the leucine side chains from one alpha helix interdigitate with those from the alpha helix of a second polypeptide, facilitating dimerization. (wikipedia.org)
  • Leucine zipper is created by the dimerization of two specific alpha helix monomers bound to DNA. (wikipedia.org)
  • This region of the alpha-helix- containing the leucines which line up- is called a ZIP domain, and leucines from each ZIP domain can weakly interact with leucines from other ZIP domains, reversibly holding their alpha-helices together (dimerization). (wikipedia.org)
  • They are characterized by a 60-80 amino acid bZIP domain: a basic DNA binding domain followed by a leucine zipper dimerization domain. (neighborshateus.com)
  • The Leucine Zipper and the Basic DNA-Binding Domain (bZIP) This leucine zipper facilitates the dimerization of the protein by interdigitation of two leucine containing helices on different molecules and these residues form the buried subunit interface of the coiled-coil dimer. (neighborshateus.com)
  • When these alpha helices dimerize, the zipper is formed. (wikipedia.org)
  • They were first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-amino acid segment and the display of these amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. (wikipedia.org)
  • Max is a basic helix-loop-helix/leucine zipper (bHLH/LZ) protein that forms sequence-specific DNA-binding complexes with the c-Myc oncoprotein (Myc). (ox.ac.uk)
  • With apolar amino acid residues at either the e or g position, a heterotetramer consisting of 2 different leucine zippers can be generated in-vitro, which implies that the overall hydrophobicity of the interaction surface and van der Waals interaction may alter the organization of coiled coils and play a role in the formation of leucine zipper heterodimer. (wikipedia.org)
  • Since most of the heptadic leucines are also conserved in the corresponding domains of other paramyxoviruses like rinderpest, measels, SV5 and para-influenza, it may indicate a similar role of this domain in these viruses as welt. (tau.ac.il)
  • Two different types of such a-helices can pair up to form a heterodimeric leucine zipper. (wikipedia.org)
  • Leucine, an essential amino acid, is one of the three amino acid with a branched hydrocarbon side chain. (neighborshateus.com)
  • In the case of leucine zippers, leucines are predominant at the d position of the heptad repeat. (wikipedia.org)
  • Leucines occurring in heptad repeats end up on the same sides of the helixes and are adjacent to each other in the stem of the Y (the "zipper" region). (bvsalud.org)