3O40
Complex of a chimeric alpha/beta-peptide based on the gp41 CHR domain bound to gp41-5
3O40 の概要
| エントリーDOI | 10.2210/pdb3o40/pdb |
| 関連するPDBエントリー | 3O3X 3O3Y 3O3Z 3O42 3O43 |
| 分子名称 | gp41-5, chimeric alpha/beta peptide based on gp41 CHR domain sequence, GLYCEROL, ... (6 entities in total) |
| 機能のキーワード | hiv fusion inhibitor, mixed alpha-peptide/beta-peptide backbone, viral protein |
| 由来する生物種 | artificial gene 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 27464.07 |
| 構造登録者 | |
| 主引用文献 | Johnson, L.M.,Horne, W.S.,Gellman, S.H. Broad Distribution of Energetically Important Contacts across an Extended Protein Interface. J.Am.Chem.Soc., 133:10038-10041, 2011 Cited by PubMed 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. PubMed: 21644542DOI: 10.1021/ja203358t 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






