4CAH

Structure of inner DysF domain of human dysferlin

Summary for 4CAH

Entry DOI	10.2210/pdb4cah/pdb
Related	4CAI
Descriptor	DYSFERLIN, PHOSPHATE ION (3 entities in total)
Functional Keywords	membrane protein, membrane repair, limb-girdle muscular dystrophy, dysf domain
Biological source	HOMO SAPIENS (HUMAN)
Cellular location	Cell membrane, sarcolemma; Single-pass type II membrane protein: O75923
Total number of polymer chains	1
Total formula weight	13888.06
Authors	Sula, A.,Cole, A.R.,Yeats, C.,Orengo, C.,Keep, N.H. (deposition date: 2013-10-08, release date: 2014-01-29, Last modification date: 2023-12-20)
Primary citation	Sula, A.,Cole, A.R.,Yeats, C.,Orengo, C.,Keep, N.H. Crystal Structures of the Human Dysferlin Inner Dysf Domain Bmc Struct.Biol., 14:3-, 2014 Cited by PubMed Abstract: Mutations in dysferlin, the first protein linked with the cell membrane repair mechanism, causes a group of muscular dystrophies called dysferlinopathies. Dysferlin is a type two-anchored membrane protein, with a single C terminal trans-membrane helix, and most of the protein lying in cytoplasm. Dysferlin contains several C2 domains and two DysF domains which are nested one inside the other. Many pathogenic point mutations fall in the DysF domain region. PubMed: 24438169 DOI: 10.1186/1472-6807-14-3 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.901 Å)

Structure validation