Abstract:
:Plasminogen activator inhibitor-1 (PAI-1) is a serine protease inhibitor (serpin) that plays an important role in cardiovascular disorders and tumor development. The potential role of PAI-1 as a drug target has been evaluated in various animal models (e.g. mouse and rat). Sensitivity to PAI-1 inhibitory agents varied in different species. To date, absence of PAI-1 structures from species other than human hampers efforts to reveal the molecular basis for the observed species differences. Here we describe the structure of latent mouse PAI-1. Comparison with available structures of human PAI-1 reveals (1) a differential positioning of α-helix A; (2) differences in the gate region; and (3) differences in the reactive center loop position. We demonstrate that the optimal binding site of inhibitors may be dependent on the orthologs, and our results affect strategies in the rational design of a pharmacologically active PAI-1 inhibitor.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Dewilde M,Van De Craen B,Compernolle G,Madsen JB,Strelkov S,Gils A,Declerck PJdoi
10.1016/j.jsb.2010.03.006subject
Has Abstractpub_date
2010-07-01 00:00:00pages
95-101issue
1eissn
1047-8477issn
1095-8657pii
S1047-8477(10)00083-3journal_volume
171pub_type
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