Proteomics

Dataset Information

0

A2M Q975C and C3 Q1013C disulfide mutants


ABSTRACT: Mutant A2M and C3 with disulfides replacing their thiol esters were disulfide mapped via pepsin digests.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Seandean Harwood  

LAB HEAD: Jan J. Enghild

PROVIDER: PXD019082 | Pride | 2021-02-18

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20200113_A2M_Q975C_TCEP_pepsin_1.raw Raw
20200113_A2M_Q975C_pepsin_1.raw Raw
20200113_C3_Q1013C_TCEP_pepsin_2.raw Raw
20200113_C3_Q1013C_pepsin_2.raw Raw
Rawdataonly.txt Txt
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Publications

Substituting the Thiol Ester of Human A2M or C3 with a Disulfide Produces Native Proteins with Altered Proteolysis-Induced Conformational Changes.

Harwood Seandean Lykke SL   Nielsen Nadia Sukusu NS   Pedersen Henrik H   Kjøge Katarzyna K   Nielsen Peter Kresten PK   Andersen Gregers Rom GR   Enghild Jan J JJ  

Biochemistry 20201210 51


Most proteins in the α-macroglobulin (αM) superfamily contain reactive thiol esters that are required for their biological function. Here, we have characterized the human α2-macroglobulin (A2M) and complement component C3 mutants A2M Q975C and C3 Q1013C, which replace the CGEQ thiol ester motifs of the original proteins with the disulfide-forming sequence CGEC. Mass spectrometry showed that the intended disulfide was formed in both proteins. The correct folding and native conformation of A2M Q97  ...[more]

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