Ng, H. Q., Li, Q., & Kang, C. (2022). 1H, 13C and 15N resonance assignments of the first BIR domain of cellular inhibitor of apoptosis protein 1. Biomolecular NMR Assignments, 16(1), 91–95. https://doi.org/10.1007/s12104-022-10065-8
Abstract:
Cellular inhibitor of apoptosis protein-1 (cIAP-1) is member of inhibitor of apoptosis proteins (IAPs) which can affect apoptosis through interactions with caspases. cIAP-1 is a multi-domain protein and able to regulate apoptosis through interactions with proteins such as caspases and possesses E3 ligase activity. Human cIAP-1 contains three baculovirus IAP repeat (BIR) domains which are critical for protein-protein interactions. Here, we report NMR resonance assignments of the first BIR domain of human cIAP. Its secondary structures in solution were determined based on the assigned resonances. The dynamics of this domain was obtained, and our hydrogen-deuterium exchange experiment reveals that the first helix in BIR1 is exposed to the solvent. The availability of assignments of backbone and side chain resonances will be useful for probing protein-protein interactions.
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Funding Info:
This research is supported by core funding from: 1Experimental Drug Development Centre (EDDC)
Grant Reference no. : N. A.
This research / project is supported by the Ministry of Health’s (MOH) / National Medical Research Council (NMRC) - Open Fund Individual Research Grant
Grant Reference no. : OFIRG19may-0011
Funds from the “Hundred-Talent Program” (Grant Numbers: 2020GDASYL-20200102010 and 2020GDASYL-20200102009) from Guangdong Academy of Sciences, China.
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This version of the article has been accepted for publication, after peer review and is subject to Springer Nature’s AM terms of use, but is not the Version of Record and does not reflect post-acceptance improvements, or any corrections. The Version of Record is available online at: http://dx.doi.org/10.1007/s12104-022-10065-8