8OXZ
Rat alpha5beta1 integrin, headpiece
Summary for 8OXZ
| Entry DOI | 10.2210/pdb8oxz/pdb |
| EMDB information | 17269 |
| Descriptor | Integrin subunit alpha 5, Integrin beta-1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | integrin, glycoprotein, membrane protein, cell adhesion |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 209931.92 |
| Authors | Roderer, D.,Dransart, E.,Shafaq-Zadah, M.,Bartels, R.,Johannes, L. (deposition date: 2023-05-03, release date: 2024-11-13, Last modification date: 2025-11-26) |
| Primary citation | Shafaq-Zadah, M.,Dransart, E.,Hamitouche, I.,Wunder, C.,Chambon, V.,Valades-Cruz, C.A.,Leconte, L.,Sarangi, N.K.,Robinson, J.,Bai, S.K.,Regmi, R.,Di Cicco, A.,Hovasse, A.,Bartels, R.,Nilsson, U.J.,Cianferani-Sanglier, S.,Leffler, H.,Keyes, T.E.,Levy, D.,Raunser, S.,Roderer, D.,Johannes, L. Spatial N-glycan rearrangement on alpha 5 beta 1 integrin nucleates galectin-3 oligomers to determine endocytic fate. Nat Commun, 16:9461-9461, 2025 Cited by PubMed Abstract: Membrane glycoproteins frequently adopt different conformations when altering between active and inactive states. Here, we discover a molecular switch that exploits dynamic spatial rearrangements of N-glycans during such conformational transitions to control protein function. For the conformationally switchable cell adhesion glycoprotein αβ integrin, we find that only the bent-closed state arranges N-glycans to nucleate the formation of up to tetrameric oligomers of the glycan-binding protein galectin-3. We propose a structural model of how these galectin-3 oligomers are built and how they clamp the bent-closed state to select it for endocytic uptake and subsequent retrograde trafficking to the Golgi for polarized distribution in cells. Our findings reveal the dynamic regulation of the glycan landscape at the cell surface to achieve oligomerization of galectin-3. Galectin-3 oligomers are thereby identified as functional decoders of defined spatial patterns of N-glycans on specifically the bent-closed conformational state of αβ integrin and possibly other integrin family members. PubMed: 41145507DOI: 10.1038/s41467-025-64523-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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