This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bhd
From Proteopedia
Revision as of 08:11, 20 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | UTRN, DMDL (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN
Overview
Utrophin is a close homologue of dystrophin, the protein defective in Duchenne muscular dystrophy. Like dystrophin, it is composed of three regions: an N-terminal region that binds actin filaments, a large central region with triple coiled-coil repeats, and a C-terminal region that interacts with components in the dystroglycan protein complex at the plasma membrane. The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin-binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin. Here, we present the 2.0 A structure of the second calponin homology domain of utrophin solved by X-ray crystallography, and compare it to the other calponin homology domains previously determined from spectrin and fimbrin.
About this Structure
1BHD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin., Keep NH, Norwood FL, Moores CA, Winder SJ, Kendrick-Jones J, J Mol Biol. 1999 Jan 22;285(3):1257-64. PMID:9887274
Page seeded by OCA on Thu Mar 20 10:11:01 2008
