Matches in SemOpenAlex for { <https://semopenalex.org/work/W2004265320> ?p ?o ?g. }
Showing items 1 to 94 of
94
with 100 items per page.
- W2004265320 endingPage "10057" @default.
- W2004265320 startingPage "10050" @default.
- W2004265320 abstract "The intestinal peptide hormone guanylin circulates mainly as its corresponding prohormone of 94 amino acids and is the first identified endogenous ligand of intestinal guanylyl cyclase C. While the prohormone is biologically inactive, it is processed to the fully functional form with 15 amino acid residues corresponding to the COOH terminus of the precursor protein. In addition to this inactivation of the hormone region, the prosequence makes an essential contribution to the disulfide-coupled folding of the hormone. On the basis of the recently determined solution structure of proguanylin, explanations for these functions of the prosequence were found, indicating that interstrand contacts between the NH2-terminal β-hairpin of the prosequence and the COOH-terminal hormone region are crucial for formation of the correct disulfide bonds of guanylin. To further investigate the role of individual disulfide bonds upon stabilization of the overall three-dimensional structure of proguanylin and to test the assumption of a direct effect of the prosequence on the structure of the hormone region, we studied the cysteine double mutant proteins proguanylin-C48S/C61S and proguanylin-C86S/C94S. Disulfide determination as well as CD and NMR spectroscopy of proguanylin-C48S/C61S reveals an essential function of the Cys48−Cys61 disulfide bond for the stability of the hydrophobic core and thereby for the stability of the overall three-dimensional structure of proguanylin. Furthermore, sequence specific resonance assignment of the second disulfide deletion mutant, proguanylin-C86S/C94S, and comparison of the NMR spectra of this protein with those of the wild-type protein demonstrate that the rigid helical core structure of proguanylin is not affected by the mutation. Additionally, analysis of the interstrand contacts between the termini reveals a direct effect of the prosequence on the conformation of the hormone region. On the basis of these results, we propose a cooperative mechanism that leads to formation of the correct disulfide pattern of guanylin." @default.
- W2004265320 created "2016-06-24" @default.
- W2004265320 creator A5009831262 @default.
- W2004265320 creator A5036767883 @default.
- W2004265320 creator A5046796025 @default.
- W2004265320 creator A5064886167 @default.
- W2004265320 date "2004-07-16" @default.
- W2004265320 modified "2023-10-17" @default.
- W2004265320 title "Role of Disulfide Bonds for the Structure and Folding of Proguanylin" @default.
- W2004265320 cites W1543394229 @default.
- W2004265320 cites W1969401721 @default.
- W2004265320 cites W1981625838 @default.
- W2004265320 cites W2002195659 @default.
- W2004265320 cites W2003116101 @default.
- W2004265320 cites W2010694921 @default.
- W2004265320 cites W2010757014 @default.
- W2004265320 cites W2035699898 @default.
- W2004265320 cites W2062739427 @default.
- W2004265320 cites W2082176639 @default.
- W2004265320 cites W2091503373 @default.
- W2004265320 cites W2130086849 @default.
- W2004265320 cites W2313422370 @default.
- W2004265320 cites W4229597618 @default.
- W2004265320 cites W4242009576 @default.
- W2004265320 cites W65749492 @default.
- W2004265320 doi "https://doi.org/10.1021/bi049667e" @default.
- W2004265320 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15287732" @default.
- W2004265320 hasPublicationYear "2004" @default.
- W2004265320 type Work @default.
- W2004265320 sameAs 2004265320 @default.
- W2004265320 citedByCount "5" @default.
- W2004265320 countsByYear W20042653202017 @default.
- W2004265320 countsByYear W20042653202021 @default.
- W2004265320 crossrefType "journal-article" @default.
- W2004265320 hasAuthorship W2004265320A5009831262 @default.
- W2004265320 hasAuthorship W2004265320A5036767883 @default.
- W2004265320 hasAuthorship W2004265320A5046796025 @default.
- W2004265320 hasAuthorship W2004265320A5064886167 @default.
- W2004265320 hasConcept C112887158 @default.
- W2004265320 hasConcept C119599485 @default.
- W2004265320 hasConcept C127413603 @default.
- W2004265320 hasConcept C178790620 @default.
- W2004265320 hasConcept C181199279 @default.
- W2004265320 hasConcept C185592680 @default.
- W2004265320 hasConcept C204328495 @default.
- W2004265320 hasConcept C27256138 @default.
- W2004265320 hasConcept C2776545253 @default.
- W2004265320 hasConcept C2779201268 @default.
- W2004265320 hasConcept C2779281246 @default.
- W2004265320 hasConcept C31684184 @default.
- W2004265320 hasConcept C32909587 @default.
- W2004265320 hasConcept C5098756 @default.
- W2004265320 hasConcept C515207424 @default.
- W2004265320 hasConcept C55493867 @default.
- W2004265320 hasConcept C71240020 @default.
- W2004265320 hasConceptScore W2004265320C112887158 @default.
- W2004265320 hasConceptScore W2004265320C119599485 @default.
- W2004265320 hasConceptScore W2004265320C127413603 @default.
- W2004265320 hasConceptScore W2004265320C178790620 @default.
- W2004265320 hasConceptScore W2004265320C181199279 @default.
- W2004265320 hasConceptScore W2004265320C185592680 @default.
- W2004265320 hasConceptScore W2004265320C204328495 @default.
- W2004265320 hasConceptScore W2004265320C27256138 @default.
- W2004265320 hasConceptScore W2004265320C2776545253 @default.
- W2004265320 hasConceptScore W2004265320C2779201268 @default.
- W2004265320 hasConceptScore W2004265320C2779281246 @default.
- W2004265320 hasConceptScore W2004265320C31684184 @default.
- W2004265320 hasConceptScore W2004265320C32909587 @default.
- W2004265320 hasConceptScore W2004265320C5098756 @default.
- W2004265320 hasConceptScore W2004265320C515207424 @default.
- W2004265320 hasConceptScore W2004265320C55493867 @default.
- W2004265320 hasConceptScore W2004265320C71240020 @default.
- W2004265320 hasIssue "31" @default.
- W2004265320 hasLocation W20042653201 @default.
- W2004265320 hasLocation W20042653202 @default.
- W2004265320 hasOpenAccess W2004265320 @default.
- W2004265320 hasPrimaryLocation W20042653201 @default.
- W2004265320 hasRelatedWork W1599103159 @default.
- W2004265320 hasRelatedWork W1993008021 @default.
- W2004265320 hasRelatedWork W2013771354 @default.
- W2004265320 hasRelatedWork W2026642912 @default.
- W2004265320 hasRelatedWork W2047754370 @default.
- W2004265320 hasRelatedWork W2051697574 @default.
- W2004265320 hasRelatedWork W2075044224 @default.
- W2004265320 hasRelatedWork W3082846984 @default.
- W2004265320 hasRelatedWork W3117136673 @default.
- W2004265320 hasRelatedWork W3185489799 @default.
- W2004265320 hasVolume "43" @default.
- W2004265320 isParatext "false" @default.
- W2004265320 isRetracted "false" @default.
- W2004265320 magId "2004265320" @default.
- W2004265320 workType "article" @default.