5GW9

Crystal structure of C163, a backbone circularized G-CSF

Summary for 5GW9

• Entry DOI: 10.2210/pdb5gw9/pdb
• Descriptor: Granulocyte colony-stimulating factor (2 entities in total)
• Functional Keywords: cytokine, four-helix bundle, backbone circulatization
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted: P09919
• Total number of polymer chains: 4
• Total formula weight: 70385.01

Authors

Miyafusa, T.,Honda, S. (deposition date: 2016-09-09, release date: 2017-09-13, Last modification date: 2024-10-30)

Primary citation

Miyafusa, T.,Shibuya, R.,Honda, S.
Structural insights into the backbone-circularized granulocyte colony-stimulating factor containing a short connector.
Biochem. Biophys. Res. Commun., 500:224-228, 2018

PubMed Abstract: Backbone circularization is a powerful approach for enhancing the structural stability of polypeptides. Herein, we present the crystal structure of the circularized variant of the granulocyte colony-stimulating factor (G-CSF) in which the terminal helical region was circularized using a short, two-amino acid connector. The structure revealed that the N- and C-termini were indeed connected by a peptide bond. The local structure of the C-terminal region transited from an α helix to 3 helix with a bend close to the N-terminal region, indicating that the structural change offset the insufficient length of the connector. This is the first-ever report of a crystal structure of the backbone of a circularized protein. It will facilitate the development of backbone circularization methodology.

PubMed: 29634929
DOI: 10.1016/j.bbrc.2018.04.045

Experimental method

X-RAY DIFFRACTION (1.65 Å)