Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation

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Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation. / Wang, Xiao Jun; Cao, Qin; Liu, Xiang; Wang, Kai Tuo; Mi, Wei; Zhang, Yan; Li, Lan Fen; Leblanc, Andrea C.; Su, Xiao Dong.

In: EMBO Reports, Vol. 11, No. 11, 01.11.2010, p. 841-847.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wang, XJ, Cao, Q, Liu, X, Wang, KT, Mi, W, Zhang, Y, Li, LF, Leblanc, AC & Su, XD 2010, 'Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation', EMBO Reports, vol. 11, no. 11, pp. 841-847. https://doi.org/10.1038/embor.2010.141

APA

Wang, X. J., Cao, Q., Liu, X., Wang, K. T., Mi, W., Zhang, Y., Li, L. F., Leblanc, A. C., & Su, X. D. (2010). Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation. EMBO Reports, 11(11), 841-847. https://doi.org/10.1038/embor.2010.141

Vancouver

Wang XJ, Cao Q, Liu X, Wang KT, Mi W, Zhang Y et al. Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation. EMBO Reports. 2010 Nov 1;11(11):841-847. https://doi.org/10.1038/embor.2010.141

Author

Wang, Xiao Jun ; Cao, Qin ; Liu, Xiang ; Wang, Kai Tuo ; Mi, Wei ; Zhang, Yan ; Li, Lan Fen ; Leblanc, Andrea C. ; Su, Xiao Dong. / Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation. In: EMBO Reports. 2010 ; Vol. 11, No. 11. pp. 841-847.

Bibtex

@article{61a8de672fff45249d7919f4ed7d7850,
title = "Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation",
abstract = "Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site 190 TEVD 193 is well structured and inserts into the active site. This positions residue Asp 193 to be easily attacked by the catalytic residue Cys 163. We demonstrate biochemically that intramolecular cleavage at Asp 193 is a prerequisite for CASP6 self-activation and that this activation mechanism is dependent on the length of the L2 loop. Our results indicate that CASP6 can be activated and regulated through intramolecular self-cleavage.",
keywords = "Alzheimer disease, apoptosis, caspase 6, cysteine protease, intramolecular cleavage",
author = "Wang, {Xiao Jun} and Qin Cao and Xiang Liu and Wang, {Kai Tuo} and Wei Mi and Yan Zhang and Li, {Lan Fen} and Leblanc, {Andrea C.} and Su, {Xiao Dong}",
year = "2010",
month = nov,
day = "1",
doi = "10.1038/embor.2010.141",
language = "English",
volume = "11",
pages = "841--847",
journal = "E M B O Reports",
issn = "1469-221X",
publisher = "Wiley-Blackwell",
number = "11",

}

RIS

TY - JOUR

T1 - Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation

AU - Wang, Xiao Jun

AU - Cao, Qin

AU - Liu, Xiang

AU - Wang, Kai Tuo

AU - Mi, Wei

AU - Zhang, Yan

AU - Li, Lan Fen

AU - Leblanc, Andrea C.

AU - Su, Xiao Dong

PY - 2010/11/1

Y1 - 2010/11/1

N2 - Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site 190 TEVD 193 is well structured and inserts into the active site. This positions residue Asp 193 to be easily attacked by the catalytic residue Cys 163. We demonstrate biochemically that intramolecular cleavage at Asp 193 is a prerequisite for CASP6 self-activation and that this activation mechanism is dependent on the length of the L2 loop. Our results indicate that CASP6 can be activated and regulated through intramolecular self-cleavage.

AB - Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site 190 TEVD 193 is well structured and inserts into the active site. This positions residue Asp 193 to be easily attacked by the catalytic residue Cys 163. We demonstrate biochemically that intramolecular cleavage at Asp 193 is a prerequisite for CASP6 self-activation and that this activation mechanism is dependent on the length of the L2 loop. Our results indicate that CASP6 can be activated and regulated through intramolecular self-cleavage.

KW - Alzheimer disease

KW - apoptosis

KW - caspase 6

KW - cysteine protease

KW - intramolecular cleavage

UR - http://www.scopus.com/inward/record.url?scp=78049347657&partnerID=8YFLogxK

U2 - 10.1038/embor.2010.141

DO - 10.1038/embor.2010.141

M3 - Journal article

C2 - 20890311

AN - SCOPUS:78049347657

VL - 11

SP - 841

EP - 847

JO - E M B O Reports

JF - E M B O Reports

SN - 1469-221X

IS - 11

ER -

ID: 234874581