6DJP
Integrin alpha-v beta-8 in complex with the Fabs 8B8 and 68
Summary for 6DJP
| Entry DOI | 10.2210/pdb6djp/pdb |
| EMDB information | 7939 |
| Descriptor | Integrin alpha-v, 2-acetamido-2-deoxy-beta-D-glucopyranose, Integrin beta-8, ... (10 entities in total) |
| Functional Keywords | glycoprotein, membrane protein, adhesion, fab |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 274901.35 |
| Authors | Cormier, A.,Campbell, M.G.,Nishimura, S.L.,Cheng, Y. (deposition date: 2018-05-25, release date: 2018-07-25, Last modification date: 2024-10-09) |
| Primary citation | Cormier, A.,Campbell, M.G.,Ito, S.,Wu, S.,Lou, J.,Marks, J.,Baron, J.L.,Nishimura, S.L.,Cheng, Y. Cryo-EM structure of the alpha v beta 8 integrin reveals a mechanism for stabilizing integrin extension. Nat. Struct. Mol. Biol., 25:698-704, 2018 Cited by PubMed Abstract: Integrins are conformationally flexible cell surface receptors that survey the extracellular environment for their cognate ligands. Interactions with ligands are thought to be linked to global structural rearrangements involving transitions between bent, extended-closed and extended-open forms. Thus far, structural details are lacking for integrins in the extended conformations due to extensive flexibility between the headpiece and legs in this conformation. Here we present single-particle electron cryomicroscopy structures of human αvβ8 integrin in the extended-closed conformation, which has been considered to be a low-affinity intermediate. Our structures show the headpiece rotating about a flexible αv knee, suggesting a ligand surveillance mechanism for integrins in their extended-closed form. Our model predicts that the extended conformation is mainly stabilized by an interface formed between flexible loops in the upper and lower domains of the αv leg. Confirming these findings with the αvβ3 integrin suggests that our model of stabilizing the extended-closed conformation is generalizable to other integrins. PubMed: 30061598DOI: 10.1038/s41594-018-0093-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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