期刊
IUCRJ
卷 6, 期 -, 页码 948-957出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S205225251901073X
关键词
X-chromosome-linked inhibitor of apoptosis protein; full-length XIAP; SAXS; EPR; integrative structural biology
资金
- iNEXT - Horizon 2020 programme of the European Union [653706, PID 2861]
- CERM/CIRMMP Italy Centre
- Instruct-ERIC, a Landmark ESFRI project
The X-chromosome-linked inhibitor of apoptosis protein (XIAP) is a multidomain protein whose main function is to block apoptosis by caspase inhibition. XIAP is also involved in other signalling pathways, including NF-kappa B activation and copper homeostasis. XIAP is overexpressed in tumours, potentiating cell survival and resistance to chemotherapeutics, and has therefore become an important target for the treatment of malignancy. Despite the fact that the structure of each single domain is known, the conformation of the full-length protein has never been determined. Here, the first structural model of the full-length XIAP dimer, determined by an integrated approach using nuclear magnetic resonance, small-angle X-ray scattering and electron paramagnetic resonance data, is presented. It is shown that XIAP adopts a compact and relatively rigid conformation, implying that the spatial arrangement of its domains must be taken into account when studying the interactions with its physiological partners and in developing effective inhibitors.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据