Home (Motif)


Home » Biology » Motif



Biology  Moss  Motor neuron

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) ...

s from the deep
Tony W Hwang*, Vlad Codrea and Andrew D Ellington
Include ...

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.

finder The 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.

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.
Related Terms:
Protein ...

s 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.

A common motif in the secondary structure of proteins, the alpha helix (α-helix) is a right-handed coiled conformation, resembling a spring, ...

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 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.
top view
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 s 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) ...

Domains often contain smaller s, 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 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.
Related Terms:
Motif ...

The basic plant cell shares a similar construction with the typical eukaryote cell, but does not have centrioles, lysosomes, intermediate filaments, cilia, or flagella, as does the animal cell.

A protein structural motif common in transcription factors. Leucine zipper is formed by two proteins (homodimmer or heterodimmer) and binds to DNA.
Other Resources
PubMed Google ...

helix- A secondary structural 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).

(a) The dominant structural of fungi (except the yeasts) is the hyphae
(b) Hyphae are long, multinucleated, typically multicelled, one-cell thick fungal tissue ...

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 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 "", ...

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 .
Biological molecules recognize and interact with one another with a specificity based on molecular shape.

See also: See also: Protein, Sequence, Trans, Proteins, Organ

Biology  Moss  Motor neuron

RSS Mobile