Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Allosteric disordering of eIF2B regulates the integrated stress response.
Journal, issue, pages	Nat Chem Biol, Year 2026
Publish date	Jun 29, 2026
Authors	Udit Dalwadi / Advait Subramanian / Aniliese Deal / Julia E Conrad / Tamara Nadjsombati / Meera Venkatesh / Morgane Boone / Pascal F Egea / Lingjie He / Nimit Jain / D John Lee / Yuwei Liu / Lucas C Reineke / Kazuki Saito / Nathaniel Talledge / Hannah Toutkoushian / Maxence Le Vasseur / Francesca Zappa / Raoul J de Groot / Diego Acosta-Alvear / Christopher P Arthur / Jodi Nunnari / Susan Marqusee / Rosalie E Lawrence / Mauro Costa-Mattioli / James J Crawford / Frank J M van Kuppeveld / Tristan I Croll / Peter Walter / Adam Frost /
PubMed Abstract	The ternary complex, composed of eIF2, GTP and initiator methionyl-tRNA, delivers the first amino acid to the ribosome to initiate protein synthesis. Eukaryotic initiation factor 2B (eIF2B) catalyzes ...The ternary complex, composed of eIF2, GTP and initiator methionyl-tRNA, delivers the first amino acid to the ribosome to initiate protein synthesis. Eukaryotic initiation factor 2B (eIF2B) catalyzes GDP to GTP exchange on eIF2, thereby setting the ternary complex level. Stress-induced phosphorylation converts eIF2 from the substrate of eIF2B into an inhibitor (eIF2-P). This conversion reduces ternary complex levels and induces the integrated stress response (ISR). Here we chart an allosteric axis running through eIF2B, revealing the importance of an α-helix in its β-subunit, the 'latch-helix', that hooks onto the α-subunit to induce eIF2B activity. eIF2-P binding promotes latch-helix unhooking, opening eIF2B, which inhibits its activity. Convergently evolved viral proteins stabilize this latch-helix-binding active state of eIF2B. Using these insights, we generated ISR-activating compounds that stabilize eIF2B in its inhibited, unlatched state. Our study thus highlights how long-range eIF2B allostery can be pharmacologically manipulated to sustain or attenuate the ISR.
External links	Nat Chem Biol / PubMed:42373951
Methods	EM (single particle)
Resolution	2.1 - 3.3 Å
Structure data	72462 9y3p EMDB-72462: Eukaryotic translation initiation factor 2-B in its apo form (active-state) (CASP target) PDB-9y3p: Eukaryotic translation initiation factor 2-B in its apo form (active-state) Method: EM (single particle) / Resolution: 2.9 Å 72463 9y3q EMDB-72463: Eukaryotic translation initiation factor 2-B in its apo form (inactive-state) (CASP target) PDB-9y3q: Eukaryotic translation initiation factor 2-B in its apo form (inactive-state) Method: EM (single particle) / Resolution: 3.3 Å 72466 9y3t EMDB-72466: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) (CASP target) PDB-9y3t: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) Method: EM (single particle) / Resolution: 2.5 Å 72467 9y3u EMDB-72467: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (inactive state) (CASP target) PDB-9y3u: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (inactive state) Method: EM (single particle) / Resolution: 2.4 Å 72468 9y3v EMDB-72468, PDB-9y3v: Eukaryotic translation initiation factor 2-B (eIF2B) bound to the viral effector AcP10 Method: EM (single particle) / Resolution: 2.9 Å 72477 9y4b EMDB-72477: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) bound to the viral effector AcP10 (CASP target) PDB-9y4b: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) bound to the viral effector AcP10 Method: EM (single particle) / Resolution: 2.1 Å 72499 9y4w EMDB-72499: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) asymmetrically bound to the viral effector AcP10 (CASP target) PDB-9y4w: Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) asymmetrically bound to the viral effector AcP10 Method: EM (single particle) / Resolution: 2.4 Å 72520 9y5r EMDB-72520, PDB-9y5r: Eukaryotic translation initiation factor 2-B (eIF2B) bound to phosphorylated eIF2alpha (NTD) Method: EM (single particle) / Resolution: 3.01 Å 72521 9y5s EMDB-72521, PDB-9y5s: eIF2B lacking the latch helix bound to ISRACT-01 (Inactive state) Method: EM (single particle) / Resolution: 3.1 Å 72522 9y5t EMDB-72522, PDB-9y5t: eIF2B lacking the latch helix bound to ISRACT-02 (Active state) Method: EM (single particle) / Resolution: 2.78 Å 72523 9y5u EMDB-72523, PDB-9y5u: eIF2B lacking the latch helix bound to ISRACT-02 (Inactive state) Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-CL: Unknown entry ChemComp-IMD: IMIDAZOLE ChemComp-ZN: Unknown entry ChemComp-PO4: PHOSPHATE ION ChemComp-MG: Unknown entry ChemComp-HOH: WATER PDB-1css: ALPHA-FLUORO ACID AND ALPHA-FLUORO AMIDE ANALOGS OF ACETYL-COA AS INHIBITORS OF OF CITRATE SYNTHASE: EFFECT OF PKA MATCHING ON BINDING AFFINITY AND HYDROGEN BOND LENGTH PDB-1csr: Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-coa as inhibitors of of citrate synthase: effect of pka matching on binding affinity and hydrogen bond length
Source	homo sapiens (human) beluga whale coronavirus sw1
Keywords	TRANSLATION / Guanine nucleotide exchange factor / GEF / initiation