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Lee, Changwook
Structural Biology of Cellular Biochemistry Lab
Research Interests
  • Cell biology, structural biology, protein biochemistry, membrane biology, cancer biology

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Crystallization and preliminary X-ray diffraction analysis of Trap1 complexed with Hsp90 inhibitors

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Title
Crystallization and preliminary X-ray diffraction analysis of Trap1 complexed with Hsp90 inhibitors
Author
Kang, Byoung HeonJeong, HanbinLee, Changwook
Issue Date
2014-12
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.70, no.12, pp.1683 - 1687
Abstract
Hsp90 is a molecular chaperone responsible for the assembly and regulation of many cellular client proteins. In particular, Trap1, a mitochondrial Hsp90 homologue, plays a pivotal role in maintaining mitochondrial integrity, protecting against apoptosis in cancer cells. The N (N-terminal)-M (middle) domain of human Trap1 was crystallized in complex with Hsp90 inhibitors (PU-H71 and BIIB-021) by the hanging-drop vapour-diffusion method at pH 6.5 and 293 K using 15% PEG 8K as a precipitant. Diffraction data were collected from crystals of the Trap1-PU-H71 (2.7 A) and Trap1-BIIB-021 (3.1 A) complexes to high resolution at a synchrotron-radiation source. Preliminary X-ray diffraction analysis revealed that both crystals belonged to space group P41212 or P43212, with unit-cell parameters a = b = 69.2, c = 252.5 A, and contained one molecule per asymmetric unit according to Matthews coefficient calculations.
URI
https://scholarworks.unist.ac.kr/handle/201301/9783
URL
http://scripts.iucr.org/cgi-bin/paper?S2053230X14024959
DOI
10.1107/S2053230X14024959
ISSN
2053-230X
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