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2KSW

Backbone 1H, 13C, and 15N Chemical Shift Assignments for Oryctin

2KSW の概要
エントリーDOI10.2210/pdb2ksw/pdb
NMR情報BMRB: 16676
分子名称Oryctin (1 entity in total)
機能のキーワードkazal-type, protease inhibitor, hydrolase inhibitor
由来する生物種Oryctes rhinoceros (Coconut rhinoceros beetle)
タンパク質・核酸の鎖数1
化学式量合計7257.40
構造登録者
Horita, S.,Ishibashi, J.,Nagata, K.,Miyakawa, T.,Yamakawa, M.,Tanokura, M. (登録日: 2010-01-14, 公開日: 2010-07-14, 最終更新日: 2024-11-13)
主引用文献Horita, S.,Ishibashi, J.,Nagata, K.,Miyakawa, T.,Yamakawa, M.,Tanokura, M.
Isolation, cDNA cloning, and structure-based functional characterization of oryctin, a hemolymph protein from the coconut rhinoceros beetle, Oryctes rhinoceros, as a novel serine protease inhibitor
J.Biol.Chem., 285:30150-30158, 2010
Cited by
PubMed Abstract: We isolated oryctin, a 66-residue peptide, from the hemolymph of the coconut rhinoceros beetle Oryctes rhinoceros and cloned its cDNA. Oryctin is dissimilar to any other known peptides in amino acid sequence, and its function has been unknown. To reveal that function, we determined the solution structure of recombinant (13)C,(15)N-labeled oryctin by heteronuclear NMR spectroscopy. Oryctin exhibits a fold similar to that of Kazal-type serine protease inhibitors but has a unique additional C-terminal α-helix. We performed protease inhibition assays of oryctin against several bacterial and eukaryotic proteases. Oryctin does inhibit the following serine proteases: α-chymotrypsin, endopeptidase K, subtilisin Carlsberg, and leukocyte elastase, with K(i) values of 3.9 × 10(-10) m, 6.2 × 10(-10) m, 1.4 × 10(-9) m, and 1.2 × 10(-8) m, respectively. Although the target molecule of oryctin in the beetle hemolymph remains obscure, our results showed that oryctin is a novel single domain Kazal-type inhibitor and could play a key role in protecting against bacterial infections.
PubMed: 20630859
DOI: 10.1074/jbc.M110.124735
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 2ksw
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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