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Characterization of ISG65-Cd3 complex

ABSTRACT: Identification of disulfide bonds of ISG65 protein and hydrogen-deuteium exchange with mass spectrometry for characterization of protein-protein interaction area.

INSTRUMENT(S): timsTOF Pro, solariX

ORGANISM(S): Homo Sapiens (human) Trypanosoma Brucei

TISSUE(S): Cell Suspension Culture

SUBMITTER: Petr Pompach

LAB HEAD: Sebastian Zoll

PROVIDER: PXD033606 | Pride | 2023-05-10

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	C3dshort.fasta	Fasta
	HDX_C3d.ZIP	Other
	HDX_C3d.txt	Txt
	HDX_ISG65_C3d.ZIP	Other
	HDX_ISG65_C3d.txt	Txt

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Publications

Cryo-EM structures of Trypanosoma brucei gambiense ISG65 with human complement C3 and C3b and their roles in alternative pathway restriction.

Sülzen Hagen H Began Jakub J Dhillon Arun A Kereïche Sami S Pompach Petr P Votrubova Jitka J Zahedifard Farnaz F Šubrtova Adriana A Šafner Marie M Hubalek Martin M Thompson Maaike M Zoltner Martin M Zoll Sebastian S

Nature communications 20230427 1

African Trypanosomes have developed elaborate mechanisms to escape the adaptive immune response, but little is known about complement evasion particularly at the early stage of infection. Here we show that ISG65 of the human-infective parasite Trypanosoma brucei gambiense is a receptor for human complement factor C3 and its activation fragments and that it takes over a role in selective inhibition of the alternative pathway C5 convertase and thus abrogation of the terminal pathway. No deposition ...[more]

PMID: 37105991

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Insights into PH1 disease mechanisms from the analyses of the structural stability and dynamics of AGT variants

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Structural perturbation at the N-terminal domain of human phosphoglycerate kinase 1 reduces the kinetic stability and unfolding cooperativity of a two-domain enzyme

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