uu.seUppsala universitets publikationer
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Disulfide mapping of the cyclotide kalata B1: Chemical proof of the cystic cystine knot motif
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Avdelningen för farmakognosi.
2003 (Engelska)Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 278, nr 48, s. 48188-48196Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The cyclotides are a recently discovered family of plant proteins that have the fascinating structural feature of a continuous cyclic backbone and, putatively, a knotted arrangement of their three conserved disulfide bonds. We here show definite chemical proof of the I-IV, II-V, III-VI knotted disulfide connectivity of the prototypic cyclotide kalata B1. This has been achieved by a new approach for disulfide analysis, involving partial reduction and stepwise alkylation including introduction of charges and enzymatic cleavage sites by aminoethylation of cysteines. The approach overcomes the intrinsic difficulties for disulfide mapping of cyclotides, i.e. the cyclic amide backbone, lack of cleavage sites between cysteines, and a low or clustered content of basic amino acids, and allowed a direct determination of the disulfide bonds in kalata B1 using analysis by mass spectrometry. The established disulfide connectivity is unequivocally shown to be cystine knotted by a topological analysis. This is the first direct chemical determination of disulfides in native cyclotides and unambiguously confirms the unique cyclic cystine knot motif.

Ort, förlag, år, upplaga, sidor
2003. Vol. 278, nr 48, s. 48188-48196
Nyckelord [en]
Amino Acid Motifs, Amino Acid Sequence, Chromatography; High Pressure Liquid, Conserved Sequence, Cysteine/chemistry, Disulfides, Ethylmaleimide/chemistry, Hydrogen-Ion Concentration, Ions, Molecular Sequence Data, Oldenlandia/metabolism, Peptides; Cyclic/*chemistry, Protein Folding, Spectrometry; Mass; Matrix-Assisted Laser Desorption-Ionization, Spectrum Analysis; Mass, Support; Non-U.S. Gov't, Trypsin/pharmacology
Nationell ämneskategori
Farmaceutiska vetenskaper
Identifikatorer
URN: urn:nbn:se:uu:diva-66816DOI: 10.1074/jbc.M308771200PubMedID: 12960160OAI: oai:DiVA.org:uu-66816DiVA, id: diva2:94727
Tillgänglig från: 2004-09-15 Skapad: 2004-09-15 Senast uppdaterad: 2018-01-10Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltextPubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=12960160&dopt=Citation

Personposter BETA

Göransson, Ulf

Sök vidare i DiVA

Av författaren/redaktören
Göransson, Ulf
Av organisationen
Avdelningen för farmakognosi
I samma tidskrift
Journal of Biological Chemistry
Farmaceutiska vetenskaper

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetricpoäng

doi
pubmed
urn-nbn
Totalt: 379 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf