1QAG

Actin binding region of the dystrophin homologue utrophin

Summary for 1QAG

• Entry DOI: 10.2210/pdb1qag/pdb
• Descriptor: UTROPHIN ACTIN BINDING REGION (2 entities in total)
• Functional Keywords: calponin homology domain, domain swapping, actin binding, utrophin, dystrophin, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, synapse, postsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side: P46939
• Total number of polymer chains: 2
• Total formula weight: 52224.67

Authors

Keep, N.H.,Winder, S.J.,Moores, C.A.,Walke, S.,Norwood, F.L.M.,Kendrick-Jones, J. (deposition date: 1999-03-05, release date: 2000-01-01, Last modification date: 2024-10-30)

Primary citation

Keep, N.H.,Winder, S.J.,Moores, C.A.,Walke, S.,Norwood, F.L.M.,Kendrick-Jones, J.
Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer
Structure Fold.Des., 7:1539-1546, 1999

PubMed Abstract: Utrophin is a large multidomain protein that belongs to a superfamily of actin-binding proteins, which includes dystrophin, alpha-actinin, beta-spectrin, fimbrin, filamin and plectin. All the members of this family contain a common actin-binding region at their N termini and perform a wide variety of roles associated with the actin cytoskeleton. Utrophin is the autosomal homologue of dystrophin, the protein defective in the X-linked Duchenne and Becker muscular dystrophies, and upregulation of utrophin has been suggested as a potential therapy for muscular dystrophy patients.

PubMed: 10647184
DOI: 10.1016/S0969-2126(00)88344-6

Experimental method

X-RAY DIFFRACTION (3 Å)