Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain
- Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143 (United States)
- The G. W. Hooper Foundation, Departments of Microbiology and Immunology and of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94143 (United States)
Variable packing interaction related to the conformational flexibility within the huntingtin-interacting protein 1 coiled coil domain. Huntingtin-interacting protein 1 (HIP1) is an important link between the actin cytoskeleton and clathrin-mediated endocytosis machinery. HIP1 has also been implicated in the pathogenesis of Huntington’s disease. The binding of HIP1 to actin is regulated through an interaction with clathrin light chain. Clathrin light chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding. To understand the mechanism of this conformational regulation, a high-resolution crystal structure of a stable fragment from the HIP1 coiled-coil domain was determined. The flexibility of the HIP1 coiled-coil region was evident from its variation from a previously determined structure of a similar region. A hydrogen-bond network and changes in coiled-coil monomer interaction suggest that the HIP1 coiled-coil domain is uniquely suited to allow conformational flexibility.
- OSTI ID:
- 22351203
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Vol. 66, Issue Pt 3; Other Information: PMCID: PMC2827350; PMID: 20179344; PUBLISHER-ID: mh5028; OAI: oai:pubmedcentral.nih.gov:2827350; Copyright (c) International Union of Crystallography 2010; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
Similar Records
Secondary Structure of Huntingtin Amino-Terminal Region
The actin bundling activity of actin bundling protein 34 is inhibited by calcium binding to the EF2