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1BH1

STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES

1BH1 の概要
エントリーDOI10.2210/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: 12168695
DOI: 10.1023/A:1019741202601
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1bh1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-29に公開中

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