28IY
Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1 at 2.13 Angstrom resolution
Summary for 28IY
| Entry DOI | 10.2210/pdb28iy/pdb |
| Descriptor | Kinesin light chain,C-Jun-amino-terminal kinase-interacting protein 1 isoform X2, Nanobody (3 entities in total) |
| Functional Keywords | protein complex, motor protein, nanobody, cargo recognition |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 54204.24 |
| Authors | |
| Primary citation | Peirano, E.,O'Regan, L.,Harrer, P.,Dzinovic, I.,Chegkazi, M.S.,Havrankova, P.,Brunet, T.,Capolino, R.,Cesario, C.,Ferro, S.,Hammar, E.,Ha-Vinh Leuchter, R.,Indelicato, E.,Jacob, M.,Kunc, L.,Margot, H.,Marin, O.,Mazurkiewicz-Beldzinska, M.,Mencacci, N.E.,Novelli, A.,Orec, L.,Poschmann, M.,Sitzberger, A.,Sorrentino, U.,Spanjaard, M.,Wagner, M.,Krygier, M.,Boesch, S.,Necpal, J.,Skorvanek, M.,Gilbert, D.L.,Jech, R.,Dodding, M.,Steiner, R.A.,Zech, M. Trio analysis in dystonia identifies de novo KLC1 variants in a kinesinopathy with distinct motor and neurodevelopmental features. Ebiomedicine, 129:106358-106358, 2026 Cited by PubMed Abstract: Although de novo causation in dystonia is widely acknowledged, there have been only a few trio-sequencing analyses in this field. We sought to prioritise de novo variants in dystonia and characterise the clinical and molecular features associated with the top gene candidate identified after genomic matchmaking. PubMed: 42372486DOI: 10.1016/j.ebiom.2026.106358 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.129 Å) |
Structure validation
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