Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase (Q24297624)

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English	Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase	scientific article

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scholarly article

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Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase (English)

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author name string

Alexey Dementiev

1

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József Dobó

2

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Peter G W Gettins

3

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language of work or name

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publication date

10 February 2006

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Journal of Biological Chemistry

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281

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3452-7

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6

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Serpin structure, mechanism, and function

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https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

The structure of a Michaelis serpin-protease complex

1 reference

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21 January 2018

Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism

1 reference

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21 January 2018

Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Structure of a serpin-protease complex shows inhibition by deformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Structural similarity of the covalent complexes formed between the serpin plasminogen activator inhibitor-1 and the arginine-specific proteinases trypsin, LMW u-PA, HMW u-PA, and t-PA: use of site-specific fluorescent probes of local environment

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Insight into the mechanism of serpin-proteinase inhibition from 2D [1H-15N] NMR studies of the 69 kDa alpha 1-proteinase inhibitor Pittsburgh-trypsin covalent complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

α1-Proteinase Inhibitor Forms Initial Non-covalent and Final Covalent Complexes with Elastase Analogously to Other Serpin-Proteinase Pairs, Suggesting a Common Mechanism of Inhibition

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Isolation of human erythrocyte membranes and their outer surface proteins by covalent fractionation on solid support

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

21 January 2018

Conformational stability of the covalent complex between elastase and alpha 1-proteinase inhibitor

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https://api.crossref.org/works/10.1074%2FJBC.M510564200

7 January 2021

based on heuristic

inferred from DOI database lookup

Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibility

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

7 January 2021

based on heuristic

inferred from DOI database lookup

The structure of a serpin-protease complex revealed by intramolecular distance measurements using donor-donor energy migration and mapping of interaction sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

7 January 2021

based on heuristic

inferred from DOI database lookup

Formation of a noncovalent serpin-proteinase complex involves no conformational change in the serpin. Use of 1H-15N HSQC NMR as a sensitive nonperturbing monitor of conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

7 January 2021

based on heuristic

inferred from DOI database lookup

Change in environment of the P1 side chain upon progression from the Michaelis complex to the covalent serpin-proteinase complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

7 January 2021

based on heuristic

inferred from DOI database lookup

Probing the native strain iin alpha1-antitrypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

7 January 2021

based on heuristic

inferred from DOI database lookup

Serpin-protease complexes are trapped as stable acyl-enzyme intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510564200

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1074/JBC.M510564200

1 reference

Consolidated OpenCitations Corpus – April 2017

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1 reference

https://api.fatcat.wiki/v0/release/zcqz6kpod5bi5pb3t66v3tgkru

24 November 2022

based on heuristic

mapped directly with Wikidata item

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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