9T1R
Structure of the PDZ domain of human Inturned
Summary for 9T1R
| Entry DOI | 10.2210/pdb9t1r/pdb |
| Descriptor | Protein inturned (2 entities in total) |
| Functional Keywords | pdz, gef, inturned, cytosolic protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 28703.38 |
| Authors | |
| Primary citation | Wilmes, S.,Brysch, J.,Gelze, C.,Meier, L.,Kummel, D. The planar cell polarity protein Vangl2 interacts with the PDZ-domains of Scribble but not with a unique PDZ-like domain in Inturned. Febs Lett., 2026 Cited by PubMed Abstract: The proteins Inturned and Fuzzy are members of the tri-longin domain (TLD) RabGEF family and activate the GTPase Rab23 downstream of the core planar cell polarity (PCP) proteins Vangl2 and Prickle. To gain insight into the function of a predicted PDZ domain unique to Inturned among TLD proteins, we performed structural and biochemical characterisations. We show that this domain does not interact with membranes or Vangl2. Instead, we find a phosphorylation-dependent interaction between Vangl2 and a PDZ domain of the apical-basal polarity protein Scribble. A crystal structure of Intu-PDZ reveals a unique PDZ-like fold lacking an interaction site for PDZ-binding motifs. Our data provide new insight into the role of PDZ domains in coordinating cell polarity downstream of Vangl2. PubMed: 41797376DOI: 10.1002/1873-3468.70319 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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