9ZCZ
C4 local refinement of stomatin-bound aquaporin (human)
Summary for 9ZCZ
| Entry DOI | 10.2210/pdb9zcz/pdb |
| EMDB information | 74046 |
| Descriptor | Aquaporin-1, CHOLESTEROL, PALMITIC ACID (3 entities in total) |
| Functional Keywords | membrane protein, aquaporin, spfh, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 106556.60 |
| Authors | Vallese, F.,Clarke, O.B. (deposition date: 2025-11-24, release date: 2026-02-25, Last modification date: 2026-04-29) |
| Primary citation | Vallese, F.,Li, H.,Barazzuol, L.,Cali, T.,Clarke, O.B. Stomatin encapsulates aquaporin-1 and urea transporter-B in the erythrocyte membrane. Sci Adv, 12:eaec1721-eaec1721, 2026 Cited by PubMed Abstract: Stomatin is a ubiquitous and highly expressed protein in erythrocytes, which associates with cholesterol-rich microdomains in the plasma membrane and is known to regulate the activity of multiple ion channels and transporters, but the structural basis of association with stomatin targets remains unknown. Here, we describe high-resolution structures of multiple stomatin complexes with endogenous binding partners isolated from human erythrocyte membranes, revealing that stomatin specifically associates with two membrane proteins involved in water transport and cell volume regulation, aquaporin-1 and the urea transporter SLC14A1. Together, our results reveal the structural basis of stomatin oligomerization, membrane association, and target recruitment and identify a putative role for stomatin in the regulation of osmotic balance in the erythrocyte. PubMed: 41921000DOI: 10.1126/sciadv.aec1721 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.3 Å) |
Structure validation
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