7API

THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM

「5API」から置き換えられました

7API の概要

• エントリーDOI: 10.2210/pdb7api/pdb
• 関連するPDBエントリー: 8API 9API
• 分子名称: ALPHA 1-ANTITRYPSIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: proteinase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45338.23

構造登録者

Loebermann, H.,Tokuoka, R.,Deisenhofer, J.,Huber, R. (登録日: 1988-09-08, 公開日: 1990-10-15, 最終更新日: 2024-10-30)

主引用文献

Engh, R.,Lobermann, H.,Schneider, M.,Wiegand, G.,Huber, R.,Laurell, C.B.
The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism.
Protein Eng., 2:407-415, 1989

PubMed Abstract: The S variant of the human alpha 1-antitrypsin with E-264----V, is responsible for a mild alpha 1-antitrypsin deficiency quite common in the European population. S protein specifically cleaved at the susceptible peptide bond was crystallized and its crystal structure determined and refined to 3.1 A resolution. The S variant crystallizes isomorphous to the normal M variant. The difference Fourier electron density map shows the E----V change as outstanding residual density. In addition, small structural changes of the main polypeptide chain radiate from the site of mutation and affect parts far removed from it. By the mutation, internal hydrogen bonds and salt linkages of E-264 to Y-38 and K-487, respectively, are lost. They cause the far-reaching slight distortions and are probably related to the reduced thermal stability of the S mutant. They may also be responsible for slower folding of the polypeptide chain and the clinical symptoms of alpha 1-antitrypsin deficiency. In a theoretical study by molecular dynamics methods simulations of the M and S proteins were made and the results analysed with respect to structural and dynamic properties and compared with the experimental results. There is a significant correlation between experimental and theoretical results in some respects.

PubMed: 2785270
DOI: 10.1093/protein/2.6.407

実験手法

X-RAY DIFFRACTION (3 Å)