Park Jin Hee, Park Hyun Ho
School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):435-7. doi: 10.1107/S1744309113005642. Epub 2013 Mar 28.
The CARMA1 signalosome, which is composed of CARMA1 [caspase recruitment domain (CARD) containing MAGUK protein 1], BCL10 (B-cell lymphoma 10) and MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1), is a molecular-signalling complex that performs pivotal functions in T-cell receptor (TCR) and B-cell receptor (BCR) mediated NF-κB activation. In this study, the CARD domain of human CARMA1 (CARMA1 CARD), corresponding to amino acids 14-109, was overexpressed in Escherichia coli using an engineered C-terminal His tag. CARMA1 CARD was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 3.2 Å from a crystal belonging to space group P2(1)2(1)2(1) with unit-cell parameters a = 45.73, b = 53.37, c = 91.89 Å.
CARMA1信号小体由CARMA1（含半胱天冬酶招募结构域的膜相关鸟苷酸激酶蛋白1）、BCL10（B细胞淋巴瘤10）和MALT1（黏膜相关淋巴组织淋巴瘤易位蛋白1）组成，是一种分子信号复合物，在T细胞受体（TCR）和B细胞受体（BCR）介导的NF-κB激活中发挥关键作用。在本研究中，人CARMA1的CARD结构域（CARMA1 CARD，对应于氨基酸14 - 109）使用工程化的C末端组氨酸标签在大肠杆菌中过表达。然后将CARMA1 CARD纯化至同质，并在293 K下结晶。最后，从属于空间群P2(1)2(1)2(1)、晶胞参数a = 45.73、b = 53.37、c = 91.89 Å的晶体收集到分辨率为3.2 Å的X射线衍射数据。
