ACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils

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Title
ACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils
Author(s)
Byeong-Won Kim; Yang Ouk Jung; Min Kyung Kim; Do Hoon Kwon; Si Hoon Park; Jun Hoe Kim; Yong-Boo Kuk; Sun-Joo Oh; Leehyeon Kim; Bong Heon Kim; Woo Seok Yang; Hyun Kyu Song
Publication Date
2017-03
Journal
SCIENTIFIC REPORTS, v.7, no., pp.43318 -
Publisher
NATURE PUBLISHING GROUP
Abstract
The coiled-coil (CC) domain is a very important structural unit of proteins that plays critical roles in various biological functions. The major oligomeric state of CCs is a dimer, which can be either parallel or antiparallel. The orientation of each α-helix in a CC domain is critical for the molecular function of CC-containing proteins, but cannot be determined easily by sequence-based prediction. We developed a biochemical method for assessing differences between parallel and antiparallel CC homodimers and named it ACCORD (Assessment tool for homodimeric Coiled-Coil ORientation Decision). To validate this technique, we applied it to 15 different CC proteins with known structures, and the ACCORD results identified these proteins well, especially with long CCs. Furthermore, ACCORD was able to accurately determine the orientation of a CC domain of unknown directionality that was subsequently confirmed by X-ray crystallography and small angle X-ray scattering. Thus, ACCORD can be used as a tool to determine CC directionality to supplement the results of in silico prediction. © The Author(s) 2017
URI
https://pr.ibs.re.kr/handle/8788114/3758
ISSN
2045-2322
Appears in Collections:
Center for Molecular Spectroscopy and Dynamics(분자 분광학 및 동력학 연구단) > Journal Papers (저널논문)
Files in This Item:
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