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1FQQ

SOLUTION STRUCTURE OF HUMAN BETA-DEFENSIN-2

1FQQ の概要
エントリーDOI10.2210/pdb1fqq/pdb
NMR情報BMRB: 4642
分子名称BETA-DEFENSIN-2 (1 entity in total)
機能のキーワードdefensin, solution structure, antibiotic
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数1
化学式量合計4342.27
構造登録者
Sawai, M.V.,Jia, H.P.,Liu, L.,Aseyev, V.,Wiencek, J.M.,McCray Jr., P.B.,Ganz, T.,Kearney, W.R.,Tack, B.F. (登録日: 2000-09-06, 公開日: 2001-04-11, 最終更新日: 2024-10-30)
主引用文献Sawai, M.V.,Jia, H.P.,Liu, L.,Aseyev, V.,Wiencek, J.M.,McCray Jr., P.B.,Ganz, T.,Kearney, W.R.,Tack, B.F.
The NMR structure of human beta-defensin-2 reveals a novel alpha-helical segment.
Biochemistry, 40:3810-3816, 2001
Cited by
PubMed Abstract: Human beta-defensin-2 (HBD-2) is a member of the defensin family of antimicrobial peptides. HBD-2 was first isolated from inflamed skin where it is posited to participate in the killing of invasive bacteria and in the recruitment of cells of the adaptive immune response. Static light scattering and two-dimensional proton nuclear magnetic resonance spectroscopy have been used to assess the physical state and structure of HBD-2 in solution. At concentrations of < or = 2.4 mM, HBD-2 is monomeric. The structure is amphiphilic with a nonuniform surface distribution of positive charge and contains several key structural elements, including a triple-stranded, antiparallel beta-sheet with strands 2 and 3 in a beta-hairpin conformation. A beta-bulge in the second strand occurs at Gly28, a position conserved in the entire defensin family. In solution, HBD-2 exhibits an alpha-helical segment near the N-terminus that has not been previously ascribed to solution structures of alpha-defensins or to the beta-defensin BNBD-12. This novel structural element may be a factor contributing to the specific microbicidal or chemokine-like properties of HBD-2.
PubMed: 11300761
DOI: 10.1021/bi002519d
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 1fqq
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2026-02-11に公開中

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