id:"swepub:oai:DiVA.org:umu-8572"
Sökning: id:"swepub:oai:DiVA.org:umu-8572" > The structure of a ...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03521naa a2200385 4500 | |
| 001 | oai:DiVA.org:umu-8572 | |
| 003 | SwePub | |
| 008 | 080129s2000 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-85722 URI |
| 024 | 7 | a https://doi.org/10.1016/S0969-2126(00)00121-02 DOI |
| 040 | a (SwePub)umu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Fa, Mingu Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut |
| 245 | 1 0 | a The structure of a serpin–protease complex revealed by intramolecular distance measurements using donor–donor energy migration and mapping of interaction sites |
| 264 | 1 | c 2000 |
| 338 | a print2 rdacarrier | |
| 520 | a Background: The inhibitors that belong to the serpin family are widely distributed regulatory molecules that include most protease inhibitors found in blood. It is generally thought that serpin inhibition involves reactive-centre cleavage, loop insertion and protease translocation, but different models of the serpin–protease complex have been proposed. In the absence of a spatial structure of a serpin–protease complex, a detailed understanding of serpin inhibition and the character of the virtually irreversible complex have remained controversial.Results: We used a recently developed method for making precise distance measurements, based on donor–donor energy migration (DDEM), to accurately triangulate the position of the protease urokinase-type plasminogen activator (uPA) in complex with the serpin plasminogen activator inhibitor type 1 (PAI-1). The distances from residue 344 (P3) in the reactive-centre loop of PAI-1 to residues 185, 266, 313 and 347 (P1′) were determined. Modelling of the complex using this distance information unequivocally placed residue 344 in a position at the distal end from the initial docking site with the reactive-centre loop fully inserted into β sheet A. To validate the model, seven single cysteine substitution mutants of PAI-1 were used to map sites of protease–inhibitor interaction by fluorescence depolarisation measurements of fluorophores attached to these residues and cross-linking using a sulphydryl-specific cross-linker.Conclusions: The data clearly demonstrate that serpin inhibition involves reactive-centre cleavage followed by full-loop insertion whereby the covalently linked protease is translocated from one pole of the inhibitor to the opposite one. | |
| 653 | a Cross-linking | |
| 653 | a Donor–donor energy migration | |
| 653 | a Fluorescence | |
| 653 | a Intramolecular distance | |
| 653 | a PAI-1 | |
| 653 | a serpin | |
| 700 | 1 | a Bergström, Fredriku Umeå universitet,Kemiska institutionen4 aut |
| 700 | 1 | a Hägglöf, Peteru Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut |
| 700 | 1 | a Wilczynska, Malgorzatau Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)mawi0006 |
| 700 | 1 | a Johansson, Lennart B-Åu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)lejo0007 |
| 700 | 1 | a Ny, Toru Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)tony0001 |
| 710 | 2 | a Umeå universitetb Institutionen för medicinsk kemi och biofysik4 org |
| 773 | 0 | t Structureg 8:4, s. 397-405q 8:4<397-405 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-8572 |
| 856 | 4 8 | u https://doi.org/10.1016/S0969-2126(00)00121-0 |
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