☆ 4.1 Article Proceedings Paper

3-2-1: Structural insights from stepwise shrinkage of a three-helix Fc-binding domain to a single helix

PROTEIN ENGINEERING DESIGN & SELECTION (2017)

期刊

PROTEIN ENGINEERING DESIGN & SELECTION

卷 30, 期 9, 页码 619-625

出版社

OXFORD UNIV PRESS

DOI: 10.1093/protein/gzx029

关键词

protein engineering; protein minimization; tethered helix; X-ray structure

类别

Biochemistry & Molecular Biology Biotechnology & Applied Microbiology

资金

US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
DOE Office of Biological and Environmental Research
National Institutes of Health, National Institute of General Medical Sciences [P41GM103393]
National Science Foundation
National Institutes of Health/National Institute of General Medical Sciences under NSF award [DMR-1332208]
National Institute of General Medical Sciences, National Institutes of Health [GM-103485]
NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103393] Funding Source: NIH RePORTER

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摘要

The well-studied B-domain from Staphylococcal protein A is a 59 amino acid three-helix bundle that binds the Fc portion of IgG with a dissociation constant of similar to 35 nM. The B-domain variant bearing a Gly to Ala mutation (=Z-domain) has been the subject of efforts to minimize a domain's size while retaining its function. We report X-ray crystallographic characterization of three steps in such a process using complexes with Fc: the full three-helix Z-domain, a 34 amino acid two-helix version called Z34C and a 13 amino acid single helix stabilized with an exo-helix tether, called LH1.

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