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- Schnur, Einat; Noah, Eran; Ayzenshtat, Inbal; Sargsyan, Hasmik; Inui, Tatsuya; Ding, Fa-Xiang; Arshava, Boris; Sagi, Yael; Kessler, Naama; Levy, Rina; Scherf, Tali; Naider, Fred; Anglister, Jacob
- Journal of molecular biology 2011 v.410 no.5 pp. 778-797
- Human immunodeficiency virus 1; cell membranes; models; mutation; nuclear magnetic resonance spectroscopy; phenotype; tyrosine
- ... Interaction of CC chemokine receptor 5 (CCR5) with the human immunodeficiency virus type 1 (HIV-1) gp120/CD4 complex involves its amino-terminal domain (Nt-CCR5) and requires sulfation of two to four tyrosine residues in Nt-CCR5. The conformation of a 27-residue Nt-CCR5 peptide, sulfated at Y10 and Y14, was studied both in its free form and in a ternary complex with deglycosylated gp120 and a CD4- ...
- PubMed Central:
- Williams, Simon G.; Madan, Rachit; Norris, Matthew G.S.; Archer, John; Mizuguchi, Kenji; Robertson, David L.; Lovell, Simon C.
- Journal of molecular biology 2011 v.410 no.5 pp. 1023-1034
- Human immunodeficiency virus 1; algorithms; amino acids; evolution; prediction; protein structure
- ... The high levels of sequence diversity and rapid rates of evolution of HIV-1 represent the main challenges for developing effective therapies. However, there are constraints imposed by the three-dimensional protein structure that affect the sequence space accessible to the evolution of HIV-1. Here, we present a strategy for predicting the set of possible amino acid replacements in HIV. Our approach ...