3I00

Crystal Structure of the huntingtin interacting protein 1 coiled coil domain

Summary for 3I00

• Entry DOI: 10.2210/pdb3i00/pdb
• Descriptor: Huntingtin-interacting protein 1 (2 entities in total)
• Functional Keywords: transcription
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O00291
• Total number of polymer chains: 2
• Total formula weight: 28387.44

Authors

Wilbur, J.D.,Hwang, P.K.,Brodsky, F.M.,Fletterick, R.J. (deposition date: 2009-06-24, release date: 2010-02-23, Last modification date: 2024-11-06)

Primary citation

Wilbur, J.D.,Hwang, P.K.,Brodsky, F.M.,Fletterick, R.J.
Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain.
Acta Crystallogr.,Sect.D, 66:314-318, 2010

PubMed Abstract: 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.

PubMed: 20179344
DOI: 10.1107/S0907444909054535

Experimental method

X-RAY DIFFRACTION (2.3 Å)