ISDA: 9T1R

Deposition Date 2025-10-21

Release Date 2026-05-27

Last Version Date 2026-05-27

Entry Detail

PDB ID:

9T1R

Keywords:

CYTOSOLIC PROTEIN

Title:

Structure of the PDZ domain of human Inturned

Biological Source:

Source Organism(s):

Homo sapiens (Taxon ID: 9606)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.50 Å

R-Value Free:

0.32

R-Value Work:

0.27

R-Value Observed:

0.27

Space Group:

P 1 21 1

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Protein inturned
Gene (Uniprot):INTU
Chain IDs:A (auth: B), B (auth: A)
Chain Length:131
Number of Molecules:2
Biological Source:Homo sapiens

UniProt ID:Q9ULD6

Primary Citation

The planar cell polarity protein Vangl2 interacts with the PDZ-domains of Scribble but not with a unique PDZ-like domain in Inturned.

Wilmes, S, Brysch, J, Gelze, C, Meier, L, Kummel, D.Show

Febs Lett. ? ? ? (2026)

PMID: 41797376 DOI: 10.1002/1873-3468.70319

Abstact

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.

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Primary Citation of related structures

Abstact

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