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TitleThe pore conformation of lymphocyte perforin.
Journal, issue, pagesSci Adv, Vol. 8, Issue 6, Page eabk3147, Year 2022
Publish dateFeb 11, 2022
AuthorsMarina E Ivanova / Natalya Lukoyanova / Sony Malhotra / Maya Topf / Joseph A Trapani / Ilia Voskoboinik / Helen R Saibil /
PubMed AbstractPerforin is a pore-forming protein that facilitates rapid killing of pathogen-infected or cancerous cells by the immune system. Perforin is released from cytotoxic lymphocytes, together with ...Perforin is a pore-forming protein that facilitates rapid killing of pathogen-infected or cancerous cells by the immune system. Perforin is released from cytotoxic lymphocytes, together with proapoptotic granzymes, to bind to a target cell membrane where it oligomerizes and forms pores. The pores allow granzyme entry, which rapidly triggers the apoptotic death of the target cell. Here, we present a 4-Å resolution cryo-electron microscopy structure of the perforin pore, revealing previously unidentified inter- and intramolecular interactions stabilizing the assembly. During pore formation, the helix-turn-helix motif moves away from the bend in the central β sheet to form an intermolecular contact. Cryo-electron tomography shows that prepores form on the membrane surface with minimal conformational changes. Our findings suggest the sequence of conformational changes underlying oligomerization and membrane insertion, and explain how several pathogenic mutations affect function.
External linksSci Adv / PubMed:35148176 / PubMed Central
MethodsEM (single particle)
Resolution4.0 Å
Structure data

13269

7pag

EMDB-13269, PDB-7pag:
The pore conformation of lymphocyte perforin
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • mus musculus (house mouse)
KeywordsIMMUNE SYSTEM / Pore forming protein perforin

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