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Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop

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Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop (English)

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H K Song

1

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K N Lee

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2

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K S Kwon

series ordinal

3

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M H Yu

series ordinal

4

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S W Suh

series ordinal

5

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language of work or name

English

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publication date

18 December 1995

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published in

FEBS Letters

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volume

377

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issue

2

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page(s)

150-4

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cites work

Human plasma proteinase inhibitors

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21 January 2018

What do dysfunctional serpins tell us about molecular mobility and disease?

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21 January 2018

On the size of the active site in proteases. I. Papain

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21 January 2018

The alpha 1-antitrypsin gene and its deficiency states

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21 January 2018

The Z type variation of human α1-antitrypsin causes a protein folding defect

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21 January 2018

Modeling the intact form of the alpha 1-proteinase inhibitor.

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21 January 2018

AMoRe: an automated package for molecular replacement

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21 January 2018

Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins

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stated in

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21 January 2018

Crystal structure of ovalbumin as a model for the reactive centre of serpins

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21 January 2018

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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21 January 2018

Biological implications of a 3 A structure of dimeric antithrombin

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Structural basis of latency in plasminogen activator inhibitor-1

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The intact and cleaved human antithrombin III complex as a model for serpin–proteinase interactions

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Identifiers

DOI

10.1016/0014-5793(95)01331-8

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PubMed publication ID

8543039

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ResearchGate publication ID

247015010

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(Q27732225)

Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop

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