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.
Broad Distribution of Energetically Important Contacts across an Extended Protein Interface.,Johnson LM, Horne WS, Gellman SH J Am Chem Soc. 2011 Jul 6;133(26):10038-41. Epub 2011 Jun 14. PMID:21644542[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Johnson LM, Horne WS, Gellman SH. Broad Distribution of Energetically Important Contacts across an Extended Protein Interface. J Am Chem Soc. 2011 Jul 6;133(26):10038-41. Epub 2011 Jun 14. PMID:21644542 doi:10.1021/ja203358t
