Search

BIO DESIGN

pISSN 2288-6982
eISSN 2288-7105

Article

Article

Crystallization

BioDesign 2020; 8(4): 83-86

Published online December 30, 2020

https://doi.org/10.34184/kssb.2020.8.4.83

© Korean Society for Structural Biology

Preliminary crystallographic study of CD38 in complex with isatuximab, an FDA-approved antibody drug for treating multiple myeloma

Hyun Tae Lee, Yujin Kim, Ui Beom Park, Tae Jun Jeong and Yong-Seok Heo*

Department of Chemistry, Konkuk University, Seoul 05029, Republic of Korea

Correspondence to: ysheo@konkuk.ac.kr

Received: December 7, 2020; Revised: December 18, 2020; Accepted: December 18, 2020

Abstract

CD38 is a type II transmembrane glycoprotein highly expressed in diverse hematologic malignancies including B-cell nonHodgkin lymphoma and multiple myeloma cells. CD38 overexpressed on the surface of multiple myeloma cells has been highlighted as a good target for therapeutic agents. In 2020, the US FDA approved isatuximab, an anti-CD38 monoclonal antibody, for the treatment of multiple myeloma. Here, the recombinant proteins of the ectodomain of CD38 and the Fab fragment of isatuximab were expressed, and their binding complex was purified and crystallized. The crystal diffracted to 1.90 Å resolution and belonged to the space group C2, with unit cell parameters a = 217.75, b = 43.17, c = 81.73 Å, and β = 103.75°. An asymmetric unit of the crystal contains one molecule of the complex with a VM of 2.33 Å3 Da–1 and a solvent content of 47.31%.