Prosequence-mediated disulfide coupled folding of the peptide hormones guanylin and uroguanylin.
In contrast to their prohormones the mature peptide hormones guanylin and uroguanylin are not able to fold to their native disulfide connectivities upon oxidative folding. Structural properties of both peptide hormones and their precursor proteins as well as the role of their prosequences in proper disulfide coupled folding are reviewed. In addition, the structural behavior of a proguanylin mutant that closely resembles prouroguanylin has been investigated to gain further insight into structural properties of this homologous precursor protein.
Lauber
Thomas
T
Lehrstuhl für Biopolymere, Universität Bayreuth, Universitätstrasse 30, 95447 Bayreuth, Germany.
Marx
Ute C
UC
D000595:Amino Acid Sequence; D004220:Disulfides / Q000737:chemistry*; D005768:Gastrointestinal Hormones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007536:Isomerism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D045265:Natriuretic Peptides; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D004220:Disulfides; D005768:Gastrointestinal Hormones; D045265:Natriuretic Peptides; D010455:Peptides; D011498:Protein Precursors; C072685:guanylin; C084362:uroguanylin