Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58234
Type: Artigo de periódico
Title: Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii
Author: Krauchenco, S
Nagem, RAP
da Silva, JA
Marangoni, S
Polikarpov, I
Abstract: The crystallographic structure of a novel trypsin inhibitor (CTI) from Copaifera langsdorffti 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 Angstrom 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. (C) 2004 Elsevier SAS. All rights reserved.
Subject: Kunitz-type trypsin inhibitor
quick cryo-soaking
X-ray structure
beta-trefoil fold
Copaifera langsdorfii
Country: França
Editor: Editions Scientifiques Medicales Elsevier
Rights: fechado
Identifier DOI: 10.1016/j.biochi.2004.03.004
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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