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	Three cryo-EM structures of complement C3d-bound αβ reveal an unexpected layer of dynamics for αI-containing integrin receptors.
Journal, issue, pages	Sci Adv, Vol. 12, Issue 19, Page eaea7241, Year 2026
Publish date	May 8, 2026
Authors	Josefine Lorentzen / Marlene Uglebjerg Fruergaard / Szilvia Lukácsi / Martin Høgholm Jørgensen / Timo Lambertus Gerardus van Veghel / Rasmus Kjeldsen Jensen / Krzysztof Jakub Pietrzak-Lichwa / Zsuzsa Bajtay / Václav Hořejší / Rasmus Kock Flygaard / Daan Vorselen / Simon Arnold Mortensen / Gregers Rom Andersen /
PubMed Abstract	Integrins are heterodimeric membrane proteins acting as mechanosensing receptors. Nine human α-subunits contain a ligand binding αI domain, but how ligands activate αI integrins are not understood. ...Integrins are heterodimeric membrane proteins acting as mechanosensing receptors. Nine human α-subunits contain a ligand binding αI domain, but how ligands activate αI integrins are not understood. We present cryo-EM structures of the αI integrin αβ in complex with the C3d ligand. The ligand-bound αI domain appears to have two major opposite orientations relative to the β subunit. Ligand binding induces an ordered conformation of the α internal ligand region that is tightly packed between the α β-propeller and the β βI-domain. Recognition of the internal ligand induces an open βI conformation practically identical to that of ligand-bound αI-less integrins confirming that ligand binding and signaling are coupled by a universal mechanism across all integrins. Integration of our findings with prior data allows us to propose a model for C3dg/iC3b-bound αβ in the phagocytotic cup and outline mechanistic models for external ligand-induced activation of αβ.
External links	Sci Adv / PubMed:42102216 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.17 - 3.94 Å
Structure data	54052 9rm9 EMDB-54052, PDB-9rm9: Cryo-EM structure of alphaM/beta2 headpiece complex without alphaM I-domain - the consensus map from alphaM/beta2:C3d-anti-CR3-Nb headpiece complex Method: EM (single particle) / Resolution: 2.6 Å 54053 9rma EMDB-54053, PDB-9rma: Cryo-EM structure of alphaM I-domain:C3d-anti-CR3-Nb complex focused refinement from the alphaM/beta2:C3d-anti-CR3-Nb headpiece complex Method: EM (single particle) / Resolution: 3.94 Å 55521 9t3y EMDB-55521, PDB-9t3y: Cryo-EM structure of alphaM/beta2:C3d-anti-CR3-Nb headpiece complex (HPO2 3D class reconstruction) Method: EM (single particle) / Resolution: 3.44 Å 55596 9t5v EMDB-55596, PDB-9t5v: Cryo-EM structure of alphaM/beta2:C3d-anti-CR3-Nb headpiece complex (HPO1 3D class reconstruction) Method: EM (single particle) / Resolution: 3.06 Å 55597 9t5w EMDB-55597, PDB-9t5w: Cryo-EM structure of mutant R61H alphaM/beta2 headpiece complex Method: EM (single particle) / Resolution: 2.74 Å 55599 9t5z EMDB-55599, PDB-9t5z: Cryo-EM structure of alphaM/beta2:MEM148-Fab headpiece complex (without alphaM I-domain) Method: EM (single particle) / Resolution: 3.1 Å PDB-9gmu: Structure ofhuman aM ligand binding domain in complex with the aCR3 nanobody Method: X-RAY DIFFRACTION / Resolution: 3.8 Å PDB-9hll: murine aM I-domain in complex with nanobody aCR3 Method: X-RAY DIFFRACTION / Resolution: 2.17 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-SO4: SULFATE ION ChemComp-HOH: WATER ChemComp-CA: Unknown entry ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-MN: Unknown entry
Source	homo sapiens (human) lama glama (llama) mus musculus (house mouse)
Keywords	IMMUNE SYSTEM / integrin receptor / ligand binding domain / antibody / VHH / complement / phagocytosis / integrin / opsonisation