7QRW

Crystal structure of NHL domain of TRIM3

Summary for 7QRW

• Entry DOI: 10.2210/pdb7qrw/pdb
• Descriptor: Isoform 4 of Tripartite motif-containing protein 3, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: e3, trim, trim3, nhl domain, ligase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 30729.05

Authors

Chaikuad, A.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2022-01-12, release date: 2022-05-04, Last modification date: 2024-01-31)

Primary citation

Chaikuad, A.,Zhubi, R.,Tredup, C.,Knapp, S.
Comparative structural analyses of the NHL domains from the human E3 ligase TRIM-NHL family.
Iucrj, 9:720-727, 2022

PubMed Abstract: Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of the RING-type E3 ubiquitin ligases that play a role in diverse processes from homeostasis and immune response to viral restriction. While TRIM proteins typically harbor an N-terminal RING finger, a B-box and a coiled-coil domain, a high degree of diversity lies in their C termini that contain diverse protein interaction modules, most of which, both structures and their roles in intermolecular interactions, remain unknown. Here, high-resolution crystal structures of the NHL domains of three of the four human TRIM-NHL proteins, namely TRIM2, TRIM3 and TRIM71, are presented. Comparative structural analyses revealed that, despite sharing an evolutionarily conserved six-bladed β-propeller architecture, the low sequence identities resulted in distinct properties of these interaction domains at their putative binding sites for macromolecules. Interestingly, residues lining the binding cavities represent a hotspot for genetic mutations linked to several diseases. Thus, high sequence diversity within the conserved NHL domains might be essential for differentiating binding partners among TRIM-NHL proteins.

PubMed: 36381143
DOI: 10.1107/S2052252522008582

Experimental method

X-RAY DIFFRACTION (1.7 Å)