Role of disulfide bonds in the structure and activity of human insulin
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chang, SG | - |
dc.contributor.author | Choi, KD | - |
dc.contributor.author | Jang, SH | - |
dc.contributor.author | Shin, HC | - |
dc.date.available | 2018-05-08T12:56:42Z | - |
dc.date.created | 2018-04-17 | - |
dc.date.issued | 2003-12 | - |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.uri | http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/6173 | - |
dc.description.abstract | Insulin contains two inter-chain disulfide bonds between the A and B chains (A7-B7 and A20-B19), and one intra-chain linkage in the A chain (A6-A11). To investigate the role of each disulfide bond in the structure, function and stability of the molecule, three des mutants of human insulin, each lacking one of the three disulfide bonds, were prepared by enzymatic conversion of refolded mini-proinsulins. Structural and biological studies of the three des mutants revealed that all three disulfide bonds are essential for the receptor binding activity of insulin, whereas the different disulfide bonds make different contributions to the overall structure of insulin. Deletion of the A20-B19 disulfide bond had the most substantial influence on the structure as indicated by loss of ordered secondary structure, increased susceptibility to proteolysis, and markedly reduced compactness. Deletion of the A6-A11 disulfide bond caused the least perturbation to the structure. In addition, different refolding efficiencies between the three des mutants suggest that the disulfide bonds are formed sequentially in the order A20-B19, A7-B7 and A6-A11 in the folding pathway of proinsulin. | - |
dc.publisher | SPRINGER-VERLAG SINGAPORE PTE LTD | - |
dc.relation.isPartOf | MOLECULES AND CELLS | - |
dc.subject | GROWTH-FACTOR-I | - |
dc.subject | BIOLOGICAL-ACTIVITY | - |
dc.subject | FOLDING PATHWAY | - |
dc.subject | PROINSULIN | - |
dc.subject | RECEPTOR | - |
dc.subject | PROTEIN | - |
dc.subject | BINDING | - |
dc.subject | PEPTIDE | - |
dc.subject | ANALOG | - |
dc.subject | INTERMEDIATE | - |
dc.title | Role of disulfide bonds in the structure and activity of human insulin | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | MOLECULES AND CELLS, v.16, no.3, pp.323 - 330 | - |
dc.identifier.kciid | ART001008009 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000187603900009 | - |
dc.identifier.scopusid | 2-s2.0-1442356427 | - |
dc.citation.endPage | 330 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 323 | - |
dc.citation.title | MOLECULES AND CELLS | - |
dc.citation.volume | 16 | - |
dc.contributor.affiliatedAuthor | Shin, HC | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.subject.keywordAuthor | des mutants | - |
dc.subject.keywordAuthor | disulfide bonds | - |
dc.subject.keywordAuthor | insulin analogues | - |
dc.subject.keywordAuthor | mini-proinsulins | - |
dc.subject.keywordAuthor | structure-activity relationship | - |
dc.subject.keywordPlus | GROWTH-FACTOR-I | - |
dc.subject.keywordPlus | BIOLOGICAL-ACTIVITY | - |
dc.subject.keywordPlus | FOLDING PATHWAY | - |
dc.subject.keywordPlus | PROINSULIN | - |
dc.subject.keywordPlus | RECEPTOR | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | ANALOG | - |
dc.subject.keywordPlus | INTERMEDIATE | - |
dc.description.journalRegisteredClass | scopus | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
Soongsil University Library 369 Sangdo-Ro, Dongjak-Gu, Seoul, Korea (06978)02-820-0733
COPYRIGHT ⓒ SOONGSIL UNIVERSITY, ALL RIGHTS RESERVED.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.