Doliana R, Bot S, Bonaldo P, Colombatti A
Divisione di Oncologia Sperimentale 2, CRO-IRCCS, National Cancer Institute, Aviano, Italy.
FEBS Lett. 2000 Nov 3;484(2):164-8. doi: 10.1016/s0014-5793(00)02140-2.
The N-terminal cysteine-rich domain (EMI domain) of EMILIN-1 is a new protein domain that is shared with two proteins (multimerin and EMILIN-2) and with four additional database entries. The EMI domains are always located at the N-terminus, have a common gene organization, and belong to proteins that are forming or are compatible with multimer formation. The potential role of the EMI domain in the assembly of EMILIN-1 was investigated by the two-hybrid system. No reporter gene activity was detected when EMI-1 was co-transformed with the C-terminal gC1q-1 domain excluding a head-to-tail multimerization; conversely, a strong interaction was detected when the EMI-1 domain was co-transformed with the gC1q-2 domain of EMILIN-2.
弹性微原纤维蛋白-1（EMILIN-1）的N端富含半胱氨酸结构域（EMI结构域）是一种新的蛋白质结构域，与另外两种蛋白质（多聚蛋白和弹性微原纤维蛋白-2）以及另外四个数据库条目共有。EMI结构域总是位于N端，具有共同的基因组织，并且属于正在形成或与多聚体形成兼容的蛋白质。通过双杂交系统研究了EMI结构域在弹性微原纤维蛋白-1组装中的潜在作用。当EMI-1与C端gC1q-1结构域共转化时，未检测到报告基因活性，排除了头对头多聚化；相反，当EMI-1结构域与弹性微原纤维蛋白-2的gC1q-2结构域共转化时，检测到强烈的相互作用。
