Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases. (Q41866374)

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scientific article published on December 2006

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English	Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases.	scientific article published on December 2006

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22 December 2019

Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases (English)

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22 December 2019

Vigna unguiculata

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João Arg Barbosa

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22 December 2019

Luciano Paulino da Silva

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22 December 2019

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Rozeni C L Teles

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22 December 2019

Gisele F Esteves

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22 December 2019

Ricardo B Azevedo

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22 December 2019

Manuel M Ventura

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22 December 2019

Sonia M de Freitas

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22 December 2019

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1 December 2006

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22 December 2019

Biophysical Journal

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22 December 2019

92

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22 December 2019

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22 December 2019

1638-1650

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22 December 2019

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The CCP4 suite: programs for protein crystallography

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Molecular mechanism of dimerization of Bowman-Birk inhibitors. Pivotal role of ASP76 in the dimerzation

1 reference

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Human genetic diseases of proteolysis

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Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds

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Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation

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Surprising similarities in structure comparison

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Formation, crystallization, and preliminary crystallographic data of the ternary complex of alpha-chymotrypsin, beta-trypsin, and the Bowman-Birk inhibitor

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Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors

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Trypsin and chymotrypsin inhibitor of Vigna unguiculata seeds--involvement of tyrosyls in its interaction with proteases

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Identifiers

10.1529/BIOPHYSJ.106.090555

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22 December 2019

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22 December 2019

PubMed publication ID

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22 December 2019

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