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Mar 2, 2017 · 5V1D. PubMed Abstract: PRKR-like endoplasmic reticulum kinase (PERK) is one of the major sensor proteins that detect protein folding imbalances during endoplasmic reticulum (ER) stress. However, it remains unclear how ER stress activates PERK to initiate a downstream unfolded protein response (UPR). Here, we found that PERK's luminal domain can ...
- Peng Wang, Peng Wang, Jingzhi Li, Jiahui Tao, Bingdong Sha
- 2018
5v1d (database links: RCSB PDB PDBe PDBj PDBsum) Title: Complex structure of the bovine PERK luminal domain and its substrate peptide: Assembly ID: 2: Resolution: 2.799Å: Method of structure determination: X-RAY DIFFRACTION: Number of inter-chain contacts: 103: Sequence identity between the two chains: 0.984: PubMed citation: 29386355
5V1D Download: MMDB ID: 159112: PDB Deposition Date: 2017/3/2: Updated in MMDB: 2018/12: Experimental Method: x-ray diffraction. Resolution: 2.799 Å ...
Feb 14, 2018 · 5v1d: The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.
5V1D: Complex structure of the bovine PERK luminal domain and its substrate peptide
Authors: P.Wang,J.Li,B.Sha Key ref: P.Wang et al. (2018). The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.
Mar 2, 2017 · PDB Entry - 5V1D (Status - Released) Summary information: Title: Complex structure of the bovine PERK luminal domain and its substrate peptide.