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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 DOI10.2210/pdb28iy/pdb
DescriptorKinesin light chain,C-Jun-amino-terminal kinase-interacting protein 1 isoform X2, Nanobody (3 entities in total)
Functional Keywordsprotein complex, motor protein, nanobody, cargo recognition
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains2
Total formula weight54204.24
Authors
Peirano, E.,Chegkazi, M.S.,Steiner, R.A. (deposition date: 2026-02-02, release date: 2026-09-23)
Primary citationPeirano, 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: 42372486
DOI: 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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PDB entries from 2026-10-14

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