9D58
Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation
Summary for 9D58
| Entry DOI | 10.2210/pdb9d58/pdb |
| Descriptor | Dystrophin (2 entities in total) |
| Functional Keywords | actin-binding domain, tandem calponin homology domain, dystrophin, duchenne muscular dystrophy, dmd, cytoskeleton, structural protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 114293.25 |
| Authors | Streeter, O.,Shi, K.,Ervasti, J.M.,Evans III, R.L.,Muretta, J.M. (deposition date: 2024-08-13, release date: 2025-03-12) |
| Primary citation | Streeter, O.,Shi, K.,Vavra, J.,Aihara, H.,Ervasti, J.M.,Evans 3rd, R.,Muretta, J.M. Human dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation. Acta Crystallogr D Struct Biol, 81:122-129, 2025 Cited by PubMed Abstract: The structure of the N-terminal actin-binding domain of human dystrophin was determined at 1.94 Å resolution. Each chain in the asymmetric unit exists in a `closed' conformation, with the first and second calponin homology (CH) domains directly interacting via a 2500.6 Å interface. The positioning of the individual CH domains is comparable to the domain-swapped dimer seen in previous human dystrophin and utrophin actin-binding domain 1 structures. The CH1 domain is highly similar to the actin-bound utrophin structure and structural homology suggests that the `closed' single-chain conformation opens during actin binding to mitigate steric clashes between CH2 and actin. PubMed: 40007458DOI: 10.1107/S2059798325001457 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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