Broad distribution of energetically important contacts across an extended protein interface

Lisa M. Johnson, W. Seth Horne, Samuel H. Gellman

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

Infection of cells by HIV depends upon profound structural rearrangements within the trimeric viral protein gp41. Critical to this process is the formation of a six-helix bundle in which a set of three N-terminal heptad repeat (NHR) helices assemble to form a core displaying long grooves that provide docking sites for three C-terminal heptad repeat (CHR) helices. We report experiments designed to discriminate between two alternative hypotheses regarding the source of affinity between individual CHR helices and the complementary groove: (1) affinity is dominated by interactions of a small cluster of side chains at one end of the CHR helix; or (2) affinity depends upon interactions distributed across the long CHR helix. We have employed two complementary experimental designs, and results from both favor the latter hypothesis.

Original languageEnglish (US)
Pages (from-to)10038-10041
Number of pages4
JournalJournal of the American Chemical Society
Volume133
Issue number26
DOIs
StatePublished - Jul 6 2011

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