In proteins, a structural unit exhibiting a particular three-dimensional architecture that is found in a variety of proteins and usually is associated with a particular function. (Figure 3-9) ...
Motifs, themes and thematic maps of an integrated Saccharomyces cerevisiae interaction network ...
Motif over-representation analysis with shuffled matrices
To assess the probability of a PWM's predictions being enriched within as many datasets as observed with the zinger PWMs, we shuffled the PFMs of the zingers and fit a distribution to the results.
A small portion of a protein (typically less than 20 amino acids) that is homologous to regions in other proteins that perform a similar function.
See Multipilicity Of Infection.
Motif finder The Motif finder is used to find six base pair stretches (6-mers) that are over-represented within a given set of upstream sequences. It can be used to identify potential cis-regulatory sequences in a set of genes.
A meaningful pattern of nucleotides or amino acids that is shared by two or more molecules.
Multigene Locus ...
Three-dimensional structure of gene product (protein) with known or implied function. eg DNA binding membrane spanning. A motif is often inferred from a cDNA sequence.
Motifs are simple combinations of secondary structure that occur in many different proteins and which carry out a similar function. An example is the helix-loop helix. It consists of two antiparallel helices at about a 60-degree angle to each other connected by a loop.
A common motif in the secondary structure of proteins, the alpha helix (α-helix) is a right-handed coiled conformation, resembling a spring, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier ( hydrogen bonding).
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "DNA sequence".
DNA binding motif: Common sites on different proteins which facilitate their binding to DNA. Examples are leucine zipper and zinc finger proteins. Any such protein is called DNA-binding protein.
A protein binding motif that contain ~7 regions ~40 aa long containing a conserved W & D. Below is a picture of a WD40 region of Human Groucho/Tle1 (1GXR) from L. H. Pearl, S. M. Roe, L. M. Pickles.
side view ...
Leucine zipper: A motif found in certain proteins in which Leu residues are evenly spaced through an a-helical region, such that they would end up on the same face of the helix. Dimers can form between two such proteins.
Protein sequence analysis at UCL: Our research concerns protein sequence analysis, primarily exploiting the technique of protein `fingerprinting' (which uses conserved motifs to characterise particular folds and functionalities).
Helix-turn-helix motifs (← links)
Organelles (← links)
Starter trna (← links)
Eukaryote (← links)
Secretory protein (← links)
Archaea (← links)
Archaebacteria (← links)
Messenger rnas (← links)
Organelle (← links)
Chaperone (← links)
Chaperonin (← links) ...
Domains often contain smaller motifs, consisting of a conserved pattern of amino acids, or of combinations of structural elements formed by the folding of nearby amino acid sequences. An example of a motif is a helix-loop-helix, which binds to DNA.
Very high repetitions (from 1,000 to over 100,000 copies) of a basic motif or repeat unit (commonly 100 - 300 base pairs) which occur at a few loci on the genome.
Three-dimensional structure of gene product (protein) with known or implied function.
The basic plant cell shares a similar construction motif with the typical eukaryote cell, but does not have centrioles, lysosomes, intermediate filaments, cilia, or flagella, as does the animal cell.
Homeobox. A DNA sequence motif found in the coding region of many regulatory genes; the encoded amino acid structure has a helix-loop-helix structure.
Homeotic (HOX) gene. Any of a group of genes in which mutation results in the replacement of one body structure by another body structure.
A protein structural motif common in transcription factors. Leucine zipper is formed by two proteins (homodimmer or heterodimmer) and binds to DNA.
PubMed Google ...
helix- A secondary structural motif of proteins in which a linear sequence of amino acids folds into a right-handed helix stabilized by internal hydrogen bonding between backbone atoms.
Autoregulatory loops: In this type of regulatory motif, a transcription factor binds to regulatory sequences that regulate its own transcription. Such interactions can be positive (amplifying) or negative (squelching).
Double-stranded helix - A common structural motif of DNA. Two linear strands of single-stranded DNA fold into a helical shape stabilized internally by hydrogen bonds between complementary base pairs.
where the subscripts indicate the number of residues present. The motif is named for the finger-like loop of amino acids that protrudes from the zinc binding site (known as the "Cys₂/His₂ finger" (pronounced "siss-two-hiss-two").
Sara O. Dionne1, Douglas F. Lake, William J. Grimes and Margaret H. Smith, Identification of HLA-Cw6.02 and -Cw7.01 allele-specific binding motifs by screening synthetic peptide libraries. Immunogenetics 56, 391-399 (2004).
A small portion of a gene or protein that appears in many genes or proteins that are related in structure; the box usually has some specific function, sometimes called a "motif", like binding DNA or interacting with specific proteins or other molecules.
Miniature Inverted-repeat Transposable Elements (MITEs)
The recent completion of the genome sequence of rice and C. elegans has revealed that their genomes contain thousands of copies of a recurring motif consisting of ...
In these molecules, the tetrahedral shape of carbon bonded to four other atoms is often a repeating motif.
Biological molecules recognize and interact with one another with a specificity based on molecular shape.
See also: Protein, Sequence, Trans, Proteins, DNA