Caspase (CASP) are cysteine-aspartic proteases (see Protease) which function in apoptosis, necrosis and inflammation. Twelve CASP have been identified in human. CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active. The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP.

[1][2]

3D structures of caspase

Caspase 3D structures


CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, 1pyo

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3D structures of caspase3D structures of caspase

Updated on 28-April-2019

4jqy, 4jqz - hpro-CASP (mutant)

    • 1i3o - hCASP (mutant) + XIAP-BIR2
  • CASP-6
  • CASP-7
  • CASP-8
    • 5l08 – hCASP – Cryo-EM
    • 4zbw - hCASP death effector domain
    • 5h33, 5h31 - hCASP death effector domain (mutant)
    • 3kjn, 3kjq – hCASP subunit P18 + inhibitor
    • 1f9e, 1qtn, 1qdu - hCASP subunit α,β + polypeptide inhibitor
    • 1qtn, 4jj7, 4jj8, 4prz - hCASP P18, P11 + polypeptide inhibitor
    • 3h11 - hCASP (mutant) + polypeptide inhibitor
    • 2y1l - hCASP subunits P18 P10
    • 2k7z – hpro-CASP (mutant) – NMR
    • 2fun, 1i4e – CASP + P35 – Autographa californica
  • CASP-9
    • 2ar9 – hCASP (mutant)
    • 1jxq - hCASP + polypeptide inhibitor
    • 3v3k – hCASP + effector protein
    • 5wve, 5juy, 5wvc – hCASP CARD domain + APAF-1
    • 1nw9 – hCASP catalytic domain + XIAP-BIR3
    • 3ygs, 4rhw – hpro-CASP + APAF-1 CARD
  • Drosophila melanogaster CASP
    • 2fp3 – DmCASP Dronc residues 136-450 – Drosophila melanogaster
    • 3sir - DmCASP drICE residues 78-332
    • 3sip – DmCASP drICE residues 78-230 + apoptosis inhibitor
  • Metacaspase

ReferencesReferences

  1. Schweizer A, Briand C, Grutter MG. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J Biol Chem. 2003 Oct 24;278(43):42441-7. Epub 2003 Aug 14. PMID:12920126 doi:http://dx.doi.org/10.1074/jbc.M304895200
  2. Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al.. Structure and mechanism of interleukin-1 beta converting enzyme. Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875 doi:http://dx.doi.org/10.1038/370270a0

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