9EC1

The Structure of Human Dystrophin Spectrin Repeat 24

Summary for 9EC1

• Entry DOI: 10.2210/pdb9ec1/pdb
• Descriptor: Dystrophin, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: spectrin repeat, spectrin, dystrophin, duchenne muscular dystrophy, dmd, cytoskeleton, structural protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 8
• Total formula weight: 108379.72

Authors

Streeter, O.,Shi, K.,Bui, H.N.,Ervasti, J.M.,Evans III, R.L.,Muretta, J.M. (deposition date: 2024-11-13, release date: 2026-04-22, Last modification date: 2026-05-13)

Primary citation

Streeter, O.,Shi, K.,Bui, H.,Aihara, H.,Ervasti, J.M.,Evans 3rd, R.,Muretta, J.M.
The atomic structure of human dystrophin spectrin-like repeat 24.
Acta Crystallogr.,Sect.F, 82:184-193, 2026

PubMed Abstract: The structure of spectrin-like repeat 24 of human dystrophin was determined at 2.5 Å effective resolution. The structure exhibits a three-helix bundle fold, common to all spectrin-repeat family members, and shares a high degree of homology with existing structures of spectrin-like repeat 1 from dystrophin and utrophin. The structure provides molecular details of the atomic interactions that stabilize the repeat, including hydrophobic interactions and inter-helix and intra-helix salt bridges. AlphaFold models of the repeat are in excellent agreement with the structure, showing an all-atom r.m.s.d. of 1.13 Å. Accurate modeling of SR24 supports AlphaFold modeling of all 24 of the dystrophin spectrin-like repeats and the use of these models in predicting the molecular determinants of dystrophin stability, a key aspect of its biological function as a structural protein that cross-links actin filaments to the dystrophin-glycoprotein complex to mediate a mechanical connection between the cytoskeleton and the extracellular matrix.

PubMed: 42024151
DOI: 10.1107/S2053230X26003262

Experimental method

X-RAY DIFFRACTION (2.14 Å)