9NWH
Long-wavelength SAD Crystal Structure of the Third Immunoglobulin-Like Domain of Human Muscle-Specific Kinase (MuSK)
Summary for 9NWH
| Entry DOI | 10.2210/pdb9nwh/pdb |
| Descriptor | Muscle, skeletal receptor tyrosine-protein kinase, POTASSIUM ION, BROMIDE ION, ... (6 entities in total) |
| Functional Keywords | ig domain, cell surface receptor, muscle-specific kinase, neuromuscular junctions, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 10 |
| Total formula weight | 111007.91 |
| Authors | Canciani, A.,Palamini, M.,Forneris, F. (deposition date: 2025-03-22, release date: 2026-04-15, Last modification date: 2026-04-22) |
| Primary citation | Canciani, A.,Palamini, M.,Forneris, F. Molecular structure of the third immunoglobulin domain (Ig3) of human Muscle-Specific kinase (MuSK). J.Struct.Biol., 218:108320-108320, 2026 Cited by PubMed Abstract: The Muscle-Specific Kinase (MuSK) is a monotopic transmembrane receptor responsible for key signaling events during development and maintenance of neuromuscular junctions. The N-terminal extracellular portion of MuSK is characterized by multiple domains, extensively involved in molecular interactions with co-receptor LRP4 during MuSK activation. The molecular mechanisms underlying MuSK activation through self- and non-self- molecular interactions are still poorly understood. In this work, we have recombinantly produced and characterized the third Ig domain of human MuSK (hMuSK-Ig3) using X-ray crystallography. Long-wavelength experimental phasing serendipitously revealed several potassium ions bound to the ten copies of hMuSK-Ig3 found in the crystallographic asymmetric unit, arranged in a super-helical fashion with paired antiparallel inter-domain molecular contacts involving β-sheets from two neighboring molecules. Collectively, our data highlight unique structural features of this domain, including metal ion binding and surface contact hot-spots possibly suggestive of contact sites relevant for interactions with co-receptor LRP4 and/or other molecular partners involved in MuSK signaling. PubMed: 41956176DOI: 10.1016/j.jsb.2026.108320 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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