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1HDL

LEKTI domain one

1HDL の概要
エントリーDOI10.2210/pdb1hdl/pdb
関連するPDBエントリー1H0Z
NMR情報BMRB: 4910
分子名称SERINE PROTEINASE INHIBITOR LEKTI (1 entity in total)
機能のキーワードputative serine proteinase inhibitor
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6491.62
構造登録者
Lauber, T.,Roesch, P.,Marx, U.C. (登録日: 2000-11-16, 公開日: 2001-11-15, 最終更新日: 2024-11-13)
主引用文献Lauber, T.,Schulz, A.,Schweimer, K.,Adermann, K.,Marx, U.C.
Homologous Proteins with Different Folds: The Three-Dimensional Structures of Domains 1 and 6 of the Multiple Kazal-Type Inhibitor Lekti
J.Mol.Biol., 328:205-, 2003
Cited by
PubMed Abstract: We have determined the solution structures of recombinant domain 1 and native domain 6 of the multi-domain Kazal-type serine proteinase inhibitor LEKTI using multi-dimensional NMR spectroscopy. While two of the 15 potential inhibitory LEKTI domains contain three disulfide bonds typical of Kazal-type inhibitors, the remaining 13 domains have only two of these disulfide bridges. Therefore, they may represent a novel type of serine proteinase inhibitor. The first and the sixth LEKTI domain, which have been isolated from human blood ultrafiltrate, belong to this group. In spite of sharing the same disulfide pattern and a sequence identity of about 35% from the first to the fourth cysteine, the two proteins show different structures in this region. The three-dimensional structure of domain 6 consists of two helices and a beta-hairpin structure, and closely resembles the three-dimensional fold of classical Kazal-type serine proteinase inhibitors including the inhibitory binding loop. Domain 6 has been shown to be an efficient, but non-permanent serine proteinase inhibitor. The backbone geometry of its canonical loop is not as well defined as the remaining structural elements, providing a possible explanation for its non-permanent inhibitory activity. We conclude that domain 6 belongs to a subfamily of classical Kazal-type inhibitors, as the third disulfide bond and a third beta-strand are missing. The three-dimensional structure of domain 1 shows three helices and a beta-hairpin, but the central part of the structure differs remarkably from that of domain 6. The sequence adopting hairpin structure in domain 6 exhibits helical conformation in domain 1, and none of the residues within the putative P3 to P3' stretch features backbone angles that resemble those of the canonical loop of known proteinase inhibitors. No proteinase has been found to be inhibited by domain 1. We conclude that domain 1 adopts a new protein fold and is no canonical serine proteinase inhibitor.
PubMed: 12684009
DOI: 10.1016/S0022-2836(03)00245-6
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 1hdl
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2025-10-15に公開中

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