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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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API5 is a unique oncogenic, non-BIR type IAP nuclear protein and is up-regulated in several cancers. It exerts severalfunctions, such as apoptosis inhibition, cell cycle progression, cancer immune escape, and anticancer drug resistance. Although structural studies of API have revealed that API5 mediates protein-protein interactions, its detailed molecularfunctions remain unknown. Since FGF2 is one of API5’s major interacting proteins, structural studies of the API5–FGF2complex will provide insight into both proteins’ molecular function. We overexpressed and purified API5 and FGF2 inEscherichia coli and crystallized the API–FGF2 complex using polyethylene glycol (PEG) 6000 as a precipitant. Diffractiondata were collected to a 2.7 Å resolution using synchrotron X-rays. Preliminary diffraction analysis revealed that theAPI5–FGF2 complex crystal belongs to the space group P212121 with the following unit cell parameters: a = 46.862, b =76.523, c = 208.161 Å. One asymmetric unit with 49.9% solvent contains one API5-FGF2 complex. Molecular replacementcalculation, using API5 and FGF2 coordinates, provided a clear electron density map for an API5–FGF2 complex.
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