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High-resolution structures of a heterochiral coiled coil

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America
 [1];  [1];  [1];  [1];  [1];  [2];  [2];  [1];  [2];  [1];  [3];  [1]
  1. Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706,
  2. Anatrace, Maumee, OH 43537,
  3. Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706
Significance

d polypeptides represent an attractive platform for biomedical applications because of their resistance to proteolytic degradation. However, the structural principles that underlie associations between L- and D-protein partners remain poorly understood because there has been very little atomic-resolution structural characterization of such heterochiral assemblies. Here we report two X-ray crystal structures of the racemic form of an α-helical peptide derived from the influenza M2 protein. Both structures contain large heterochiral coiled–coil interfaces. The ubiquity and regularity of coiled coils has inspired extensive design effort directed toward homochiral tertiary and quaternary structures, and we anticipate that the insights from these crystal structures will facilitate the design of an analogous rich set of heterochiral proteins and assemblies.

Research Organization:
Univ. of Wisconsin, Madison, WI (United States)
Sponsoring Organization:
3M Corporation (United States); Michigan Economic Development Corporation (United States); Michigan Technology Tri-Corridor (United States); National Inst. of Health (NIH) (United States); National Oceanic and Atmospheric Administration (NOAA) (United States); National Science Foundation (NSF) (United States); USDOE; USDOE Office of Science (SC)
Contributing Organization:
Anatrace, Maumee, OH (United States)
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1235128
Alternate ID(s):
OSTI ID: 1228096
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 43 Vol. 112; ISSN 0027-8424
Publisher:
Proceedings of the National Academy of SciencesCopyright Statement
Country of Publication:
United States
Language:
English

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