Human CCL5 trimer: expression, purification and initial crystallographic studies.
Acta Crystallogr F Struct Biol Commun
; 74(Pt 2): 82-85, 2018 Feb 01.
Article
in En
| MEDLINE
| ID: mdl-29400316
ABSTRACT
The chemokine CCL5 is considered to be a potential therapeutic target because of its ability to recruit immune cells to inflammatory sites. CCL5 aggregates under physiological conditions, and high-order oligomer formation is considered to be significant for cell migration, immune-cell activation and HIV cell entry. The structure of the high-order oligomer is unknown and the mechanism by which the oligomer is derived has yet to be established. Here, a CCL5 mutant (CCL5-E66S) which is deficient in oligomer formation was mixed with native CCL5 to prepare a protein trimer. At an optimized ratio the trimeric CCL5 crystallized, and the crystal belonged to the tetragonal space group P41212, with unit-cell parameters a = 56.6, b = 56.6, c = 154.1â
Å. The Matthews coefficient (VM) of the crystal is 2.58â
Å3â
Da-1 (three molecules in the asymmetric unit), with a solvent content of 52.32%. Diffraction data were collected to a resolution of 1.87â
Å and the statistics indicated satisfactory data quality. The new structure will reveal the interfaces in the CCL5 oligomer, therefore assisting in understanding the mechanism of CCL5 oligomerization.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Sequence Analysis, DNA
/
Chemokine CCL5
/
Protein Multimerization
Limits:
Humans
Language:
En
Journal:
Acta Crystallogr F Struct Biol Commun
Year:
2018
Document type:
Article
Affiliation country:
Taiwan