pentapeptide

The pentapeptide repeat is a feature seen in protein sequence.

It includes a pentapeptide protein that should spur collagen production.

The later Bateman et al. showed that a large family of related pentapeptide repeat proteins existed.

An enkephalin is a pentapeptide involved in regulating nociception in the body.

A pentapeptide has five amino acids.

Enterostatin is a pentapeptide derived from a proenzyme in the gastrointestinal tract called procolipase.

There are five modules for cyclic pentapeptide biosynthesis, including one that lacks an adenylation domain (A).

Chrysosporide is a cyclic pentapeptide.

It has a pentapeptide structure with the amino acid sequence Val-Val-Tyr-Pro-Trp.

ADH-1 short for "Adhere" brand name Exherin, is a small, cyclic pentapeptide vascular-targeting drug.

The first crystal structure of a pentapeptide repeat protein was the MfpA protein solved by Hegde and colleagues.

Abductin is made up of three prominent amino acids, glycine, methionine, and phenylalanine, which are arranged in a repeating pentapeptide sequence throughout the molecule.

It consists of a central cyclic pentapeptide code assembled from nonribosomal peptide synthetase (NRPS).

Opiorphin pentapeptide originates from the N-terminal region of the protein PROL1 (proline rich, lacrimal 1).

The central position in the pentapeptide repeat is usually a leucine and has been designated as position i. The two previous positions are known as i-1 and i-2.

Molecular modeling and structure-activity relationship studies made it possible to pinpoint the amino acid residue of the pentapeptide inhibitor S 34461 that interacts with the cosubstrate-binding site.

This pentapeptide consists of serine (Ser) and four hydroxyprolines (Hyp): Ser-Hyp-Hyp-Hyp-Hyp.

For a protein to be a CMA substrate, it must have in its amino acid sequence a pentapeptide motif biochemically related to KFERQ.

However, in the MfpA protein a DNA gyrase inhibitor it has been suggested that the pentapeptide repeat structure mimics the structure of DNA.

Sporulation in B. subtilis is mediated by CSF (sporulation factor), a pentapeptide cleaved from the precursor peptide PhrC.

In gram-positive bacteria, the peptidoglycan molecules are cross-linked by a pentapeptide bridge, whereas in gram-negative bacteria, the peptidoglycan molecules are directly covalently bound to each other.

CdtB is functionally homologous to mammalian DNase I and contains a conserved pentapeptide sequence found in all DNase I enzymes to date.

The motif includes a conserved pentapeptide LPXTG, which precedes a hydrophobic C-terminal membrane anchor, which itself precedes a cluster of basic residues.

The core pentapeptide sequence, TTNYT, consisting of amino acids 4-8 in peptide T, is the HIV envelope sequence required for attachment to the CD4 receptor.

Colipase is secreted by the exocrine pancreas as the precursor, procolipase and its activation involves the tryptic cleavage of the Arg 5 -Gly 6 bond releasing an N terminal pentapeptide.