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The three‐dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1 H nuclear magnetic resonance
Author(s) -
Fant Franky,
Vranken Wim F.,
Borremans Frans A.M.
Publication year - 1999
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19991115)37:3<388::aid-prot7>3.0.co;2-f
Subject(s) - subfamily , aesculus hippocastanum , biology , defensin , protein structure , botany , antimicrobial , genetics , biochemistry , microbiology and biotechnology , gene
Aesculus hippocastanum antimicrobial protein 1 (Ah‐AMP1) is a plant defensin isolated from horse chestnuts. The plant defensins have been divided in several subfamilies according to their amino acid sequence homology. Ah‐AMP1, belonging to subfamily A2, inhibits growth of a broad range of fungi. So far, a three‐dimensional structure has been determined only for members of subfamilies A3 and B2. In order to understand activity and specificity of these plant defensins, the structure of a protein belonging to subfamily A2 is needed. We report the three‐dimensional solution structure of Ah‐AMP1 as determined from two‐dimensional 1 H nuclear magnetic resonance data. The structure features all the characteristics of the “cysteine‐stabilized αβ‐motif.”A comparison of the structure, the electrostatic potential surface and regions important for interaction with the fungal receptor, is made with Rs‐AFP1 (plant defensin of subfamily A3). Thus, residues important for activity and specificity have been assigned. Proteins 1999;37:388–403. ©1999 Wiley‐Liss, Inc.