Backbone and side-chain 1H, 13C and 15N assignments of the ubiquitin-associated domain of human X-linked inhibitor of apoptosis protein
| Autor: | Yinhua Yang, Sin-Kam Hui, Benjamin Chun Yu Wong, Kong-Hung Sze, Man-Kit Tse |
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| Rok vydání: | 2009 |
| Předmět: |
X-Linked Inhibitor of Apoptosis Protein
Inhibitor of apoptosis medicine.disease_cause Biochemistry Protein Structure Secondary Article Protein structure NMR spectroscopy Ubiquitin X-linked Inhibitor of Apoptosis Protein (XIAP) Structural Biology medicine Ubiquitin-associated (UBA) domain Humans Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Caspase Inhibitor of apoptosis domain Carbon Isotopes biology Nitrogen Isotopes Cell biology XIAP Resonance assignment Apoptosis biology.protein Carcinogenesis Hydrogen |
| Zdroj: | Biomolecular Nmr Assignments |
| ISSN: | 1874-270X |
| Popis: | X-linked inhibitor of apoptosis protein (XIAP), a leading member of the family of inhibitor of apoptosis (IAP) proteins, is considered as the most potent and versatile inhibitor of caspases and apoptosis. It has been reported that XIAP is frequently overexpressed in cancer and its expression level is implicated in contributing to tumorigenesis, disease progression, chemoresistance and poor patient-survival. Therefore, XIAP is one of the leading targets in drug development for cancer therapy. Recently, based on bioinformatics study, a previously unrecognized but evolutionarily conserved ubiquitin-associated (UBA) domain in IAPs was identified. The UBA domain is found to be essential for the oncogenic potential of IAP, to maintain endothelial cell survival and to protect cells from TNF-α-induced apoptosis. Moreover, the UBA domain is required for XIAP to activate NF-κB. In the present study, we report the near complete resonance assignments of the UBA domain-containing region of human XIAP protein. Secondary structure prediction based on chemical shift index (CSI) analysis reveals that the protein is predominately α-helical, which is consistent with the structures of known UBA proteins. © 2009 Springer Science+Business Media B.V. published_or_final_version Springer Open Choice, 01 Dec 2010 |
| Databáze: | OpenAIRE |
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