상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

A 2.1 Å Resolution Structure of an Uncleaved α₁-Antitrypsin Shows Variability of the Reactive Center and Other Loops

Authors 

Seung Jun KimJoo Rang WooEun Joo SeoMyeong Hee YuSeong Eon Ryu

Publisher 

Elsevier

Issue Date 

2001

Citation 

Journal of Molecular Biology, vol. 306, no. 1, pp. 109-119

Keywords 

α1-antitrypsinserpinsreactive center loopvan-der-Waals strainsurface cavity

Abstract 

Serpin (serine protease inhibitor) proteins are involved in diverse physiological processes including inflammation, coagulation, matrix remodeling, and cell differentiation. Deficiency of normal serpin functions leads to various hereditary diseases. Besides their clinical importance, serpin proteins draw much attention due to the large conformational changes that occur upon interaction with proteases. We present here the crystal structure of an uncleaved alpha(1)-antitrypsin determined by the multiple isomorphous replacement method and refined to 2.1 A resolution. The structure, which is the first active serpin structure based on experimental phases, reveals novel conformations in the flexible loops, including the proximal hinge region of the reactive center loop and the surface cavity region in the central beta-sheet, sheet A. The determined loop conformation explains the results of recent mutagenesis studies and provides detailed insights into the protease inhibition mechanism. The high-resolution structure of active alpha(1)-antitrypsin also provides evidence for the existence of localized van-der-Waals strain in the central hydrophobic core.

ISSN 

0022-2836

Link 

http://dx.doi.org/10.1006/jmbi.2000.4357

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)