5A38
Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle.
Summary for 5A38
Entry DOI | 10.2210/pdb5a38/pdb |
Related | 5A36 5A37 |
Descriptor | ALPHA-ACTININ-2 (2 entities in total) |
Functional Keywords | actin-binding protein, human alpha-actinin-2, calponin homology domains |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Cytoplasm, myofibril, sarcomere, Z line : P35609 |
Total number of polymer chains | 2 |
Total formula weight | 57173.77 |
Authors | Haywood, N.J.,Wolny, M.,Trinh, C.H.,Shuping, Y.,Edwards, T.A.,Peckham, M. (deposition date: 2015-05-27, release date: 2016-06-22, Last modification date: 2024-01-10) |
Primary citation | Haywood, N.,Wolny, M.,Rogers, B.,Trinh, C.H.,Shuping, Y.,Edwards, T.A.,Peckham, M. Hypertrophic Cardiomyopathy Mutations in the Calponin-Homology Domain of Actn2 Affect Actin Binding and Cardiomyocyte Z-Disc Incorporation. Biochem.J., 473:2485-, 2016 Cited by PubMed: 27287556DOI: 10.1042/BCJ20160421 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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