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2K51

NMR Solution Structure of the Neurotrypsin Kringle Domain

2K51 の概要
エントリーDOI10.2210/pdb2k51/pdb
関連するPDBエントリー2K4R
分子名称Neurotrypsin (1 entity in total)
機能のキーワードneurotrypsin, kringle domain, disulfide-rich protein fold, serine endopeptidase, hydrolase, extracellular proteolysis
由来する生物種Rattus norvegicus (Rat)
タンパク質・核酸の鎖数1
化学式量合計8542.46
構造登録者
Ozhogina, O.A. (登録日: 2008-06-23, 公開日: 2008-12-09, 最終更新日: 2024-10-16)
主引用文献Ozhogina, O.A.,Grishaev, A.,Bominaar, E.L.,Llinas, M.
NMR Solution Structure of the Neurotrypsin Kringle Domain
Biochemistry, 47:12290-12298, 2008
Cited by
PubMed Abstract: Neurotrypsin is a multidomain protein that serves as a brain-specific serine protease. Here we report the NMR structure of its kringle domain, NT/K. The data analysis was performed with the BACUS (Bayesian analysis of coupled unassigned spins) algorithm. This study presents the first application of BACUS to the structure determination of a 13C unenriched protein for which no prior experimental 3D structure was available. NT/K adopts the kringle fold, consisting of an antiparallel beta-sheet bridged by an overlapping pair of disulfides. The structure reveals the presence of a surface-exposed left-handed polyproline II helix that is closely packed to the core beta-structure. This feature distinguishes NT/K from other members of the kringle fold and points toward a novel functional role for a kringle domain. Functional divergence among kringle domains is discussed on the basis of their surface and electrostatic characteristics.
PubMed: 18956887
DOI: 10.1021/bi800555z
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
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件を2025-12-31に公開中

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