The CD163 long‐range scavenger receptor cysteine‐rich repeat: expression, purification and X‐ray crystallographic characterization

• Published in: Acta crystallographica. Section F, Structural biology communications Vol. 74; no. 5; pp. 322 - 326
• Main Authors: Li, Rui, Ma, Hongfang, Jiang, Longguang, Qiao, Songlin, Zhi, Yubao, Huang, Mingdong, Deng, Ruiguang, Zhang, Gaiping
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.05.2018; Wiley Subscription Services, Inc
• Subjects: Amino Acid Sequence; Antigens, CD - biosynthesis; Antigens, CD - chemistry; Antigens, CD - genetics; Antigens, Differentiation, Myelomonocytic - biosynthesis; Antigens, Differentiation, Myelomonocytic - chemistry; Antigens, Differentiation, Myelomonocytic - genetics; Cation exchanging; CD163; CD163 antigen; Crystallization - methods; Crystallography; Crystallography, X-Ray - methods; Crystals; Cysteine; Cysteine - genetics; Fruit flies; Gene Expression; long‐range scavenger receptor cysteine‐rich repeat; Potassium; Protein purification; Purification; Receptors; Receptors, Cell Surface - biosynthesis; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - genetics; Research Communications; scavenger receptor; Scavenger receptors; Single crystals; Sodium; SRCR repeat; Structure-function relationships; X‐ray crystallography; X-ray crystallography; CD163; scavenger receptor; SRCR repeat; long-range scavenger receptor cysteine-rich repeat
• ISSN: 2053-230X; 2053-230X
• DOI: 10.1107/S2053230X18005551

Scavenger receptors (SRs) play critical roles in various physiological and pathological pathways. One of them, CD163, is a multifunctional endocytic receptor and is characterized by a long‐range scavenger receptor cysteine‐rich (SRCR) repeat. However, the structural and functional details of this long‐range SRCR repeat have not yet been elucidated. In this study, the CD163 long‐range SRCR repeat was expressed in Drosophila Schneider 2 cells. The recombinant protein was homogeneous after purification by metal‐affinity, cation‐exchange and size‐exclusion chromatography. Single crystals were obtained using 20% PEG 4000, 0.15 M potassium sodium tartrate tetrahydrate pH 8.5 and diffracted to 3.30 Å resolution. As the first view of a long‐range SRCR repeat, this work lays the structural basis for a deep understanding of SRs and their multiple functions. The CD163 long‐range scavenger receptor cysteine‐rich (SRCR) repeat was prepared in a Drosophila system and was crystallized using 20% PEG 4000, 0.15 M potassium sodium tartrate tetrahydrate pH 8.5. X‐ray crystallographic characterization of this long‐range SRCR repeat will provide structural and functional information for the scavenger receptor superfamily.