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DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF AESCULUS HIPPOCASTANUM ANTIMICROBIAL PROTEIN 1 (AH-AMP1) BY 1H NMR, 25 STRUCTURESDETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF AESCULUS HIPPOCASTANUM ANTIMICROBIAL PROTEIN 1 (AH-AMP1) BY 1H NMR, 25 STRUCTURES
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAesculus 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 1H nuclear magnetic resonance data. The structure features all the characteristics of the "cysteine-stabilized alpha beta-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. The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.,Fant F, Vranken WF, Borremans FA Proteins. 1999 Nov 15;37(3):388-403. PMID:10591099[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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