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-Structure paper
タイトル | Structural and biochemical basis for induced self-propagation of NLRC4. |
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ジャーナル・号・ページ | Science, Vol. 350, Issue 6259, Page 399-404, Year 2015 |
掲載日 | 2015年10月23日 |
著者 | Zehan Hu / Qiang Zhou / Chenlu Zhang / Shilong Fan / Wei Cheng / Yue Zhao / Feng Shao / Hong-Wei Wang / Sen-Fang Sui / Jijie Chai / |
PubMed 要旨 | Responding to stimuli, nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) oligomerize into multiprotein complexes, termed inflammasomes, mediating innate immunity. ...Responding to stimuli, nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) oligomerize into multiprotein complexes, termed inflammasomes, mediating innate immunity. Recognition of bacterial pathogens by NLR apoptosis inhibitory proteins (NAIPs) induces NLR family CARD domain-containing protein 4 (NLRC4) activation and formation of NAIP-NLRC4 inflammasomes. The wheel-like structure of a PrgJ-NAIP2-NLRC4 complex determined by cryogenic electron microscopy at 6.6 angstrom reveals that NLRC4 activation involves substantial structural reorganization that creates one oligomerization surface (catalytic surface). Once activated, NLRC4 uses this surface to catalyze the activation of an inactive NLRC4, self-propagating its active conformation to form the wheel-like architecture. NAIP proteins possess a catalytic surface matching the other oligomerization surface (receptor surface) of NLRC4 but not those of their own, ensuring that one NAIP is sufficient to initiate NLRC4 oligomerization. |
リンク | Science / PubMed:26449475 |
手法 | EM (単粒子) |
解像度 | 6.7 - 25.2 Å |
構造データ | EMDB-3139: EMDB-3140: EMDB-3141: EMDB-3142: EMDB-3143: |
由来 |
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