Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii.

Abstract:

:The crystallographic structure of a novel trypsin inhibitor (CTI) from Copaifera langsdorffii is reported. The structure was solved by MIRAS procedure and refined to a crystallographic residual of 17.3% (R(free) = 20.3%) at 1.8 A resolution. Two isomorphous derivatives were obtained by quick cryo-soaking approach. CTI is the first structure of a member of Kunitz (STI) family formed by two noncovalently bound polypeptide chains and only one disulfide bridge. A standard Kunitz-type inhibitor has a single polypeptide chain and two disulfide bridges. Structural features granting CTI high inhibitory activity are discussed.

journal_name

Biochimie

journal_title

Biochimie

authors

Krauchenco S,Nagem RA,da Silva JA,Marangoni S,Polikarpov I

doi

10.1016/j.biochi.2004.03.004

keywords:

subject

Has Abstract

pub_date

2004-03-01 00:00:00

pages

167-72

issue

3

eissn

0300-9084

issn

1638-6183

pii

S0300908404000367

journal_volume

86

pub_type

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