Proline motifs in peptides and their biological processing

  title={Proline motifs in peptides and their biological processing},
  author={Greet Vanhoof and Filip Goossens and Ingrid De Meester and Dirk Hendriks and Simon Lodewijk Scharpe},
  journal={The FASEB Journal},
  pages={736 - 744}
Many biologically important peptide sequences contain proline. It confers unique conformational constraints on the peptide chain in that the side‐chain is cyclized back onto the backbone amide position. Inside an a‐helix the possibility of making hydrogen bonds to the preceding turn is lost and a kink will be introduced. The conformational restrictions imposed by proline motifs in a peptide chain appear to imply important structural or biological functions as can be deduced from their often… 

Secondary Structure as a Conformational Determinant in Processing of Peptide Precursors at Dibasic Amino Acids

The wealth of collected data point toward the conclusion that β-turns and/or loops, favored by sequences bearing basic residues, constitute a key feature in the specification of those peptide loci which are proteolytically processed in vivo.

Conformational Profile of a Proline-Arginine Hybrid

Both cis- and trans-((β)Pro)Arg exhibit a preference for the α(L) conformation as a consequence of the interactions established between the guanidinium moiety and the main-chain amide groups.

Proline specific peptidases.

Side-chain effects on peptidyl-prolyl cis/trans isomerisation.

There is a rough correlation between the cis content in the oligopeptides and the propensity of Xaa-Pro cis prolyl bonds in proteins, which suggests that the prolyL bond conformation is mainly determined by local effects in proteins.

Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer.

Structural and functional implications of a proline residue in the antimicrobial peptide gaegurin.

The observation that P14 is a more potent antibacterial agent than P14A implies that the helical kink of P14 plays an important role in the disruption of bacterial membranes.

Proline Conformation in a Functional Tau Fragment.

Processing of peptide and hormone precursors at the dibasic cleavage sites

This review focuses on the importance of privileged secondary structures and of given amino acid residues around basic cleavage sites in substrate recognition by endoproteases, a prerequisite to select which PCs are promising drug targets in each disease.



Proline-dependent structural and biological properties of peptides and proteins.

  • A. YaronF. Naider
  • Biology, Chemistry
    Critical reviews in biochemistry and molecular biology
  • 1993
A critical analysis of peptidases involved in the cleavage of proline-containing peptide bonds reveals that they may function as key pacemakers in the control of the activity of many peptide hormones and that they are involved in a variety of immunological processes, including T-cell-mediated immune response.

The structure and function of proline-rich regions in proteins.

Proline is a very unusual amino acid, in that the side-chain is cyclized back on to the backbone amide position, and the bulkiness of the N-CH2 group places restrictions on the conformation of the residue preceding proline, disfavouring the a-helix conformation.

Proline residues in transmembrane helices of channel and transport proteins: a molecular modelling study.

  • M. Sansom
  • Biology, Chemistry
    Protein engineering
  • 1992
It is shown that carbonyl oxygens exposed by the proline-induced kink and at the C-terminus of the helices may provide cation-liganding sites and implications with respect to modelling of ion channel and transport proteins are discussed.

Peptidylproline cis-trans-isomerases: immunophilins.

  • A. Galat
  • Biology
    European journal of biochemistry
  • 1993
A larger spectrum of proteins is analysed in relation to various signal-transduction pathways in lymphoid cells which involve immunophilins or their complexes with the immunosuppressants CsA, FK506 or rapamycin.

Aminopeptidase P from human leukocytes.

The observed resistance of Gly-Pro,pro-Gly, Pro-Phe and Pro-Ile to hydrolysis by the purified enzyme strongly indicates absence of known proline-specific dipeptidases in the aminopeptidase-P preparation.

Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families.

Prolylcarboxypeptidase links these two families, suggesting an evolutionary relationship, and is inhibited by benzyloxycarbonyl-Pro-prolinal, a specific inhibitor of prolylendopeptidases, another angiotensin metabolizing enzyme.