1BH1
STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES
1BH1 の概要
| エントリーDOI | 10.2210/pdb1bh1/pdb |
| NMR情報 | BMRB: 4194 |
| 分子名称 | MELITTIN (1 entity in total) |
| 機能のキーワード | toxin, hemolytic polypeptide |
| 由来する生物種 | Apis mellifera (honey bee) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 2850.49 |
| 構造登録者 | Barnham, K.J.,Hewish, D.,Werkmeister, J.,Curtain, C.,Kirkpatrick, A.,Bartone, N.,Liu, S.T.,Norton, R.,Rivett, D. (登録日: 1998-06-11, 公開日: 1999-01-06, 最終更新日: 2024-10-30) |
| 主引用文献 | Hewish, D.R.,Barnham, K.J.,Werkmeister, J.A.,Kirkpatrick, A.,Bartone, N.,Liu, S.T.,Norton, R.S.,Curtain, C.,Rivetta, D.E. Structure and activity of D-Pro14 melittin. J.Protein Chem., 21:243-253, 2002 Cited by PubMed Abstract: D-Pro14 melittin was synthesized to investigate the effect of increasing the angle of the bend in the hinge region between the helical segments of the molecule. Structural analysis by nuclear magnetic resonance indicated that, in methanol, the molecule consisted of two helices separated at Pro14, as in melittin. However, the two helices in D-Pro14 melittin were laterally displaced relative to each other by approximately 7 A, and in addition, there was a small rotation of the carboxyl-terminal helix relative to the amino-terminal helix around the long axis of the molecule. The peptide had less than 5% of the cytolytic activity of melittin. Modification of Arg22 with the 2,2,5,7,8-pentamethyl-chroman-6-sulphonyl (pmc) group restored hemolytic activity to close to that of unmodified melittin. Replacement of Arg22 with Phe was less effective in restoring hemolytic activity. Electron-paramagnetic resonance studies suggest that there is a positive correlation between hemolytic activity of the peptides and interaction with phospholipid bilayers. PubMed: 12168695DOI: 10.1023/A:1019741202601 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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