1bk8

<StructureSection load='1bk8' size='340' side='right' caption='[[1bk8]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1bk8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aesculus_hippocastanum Aesculus hippocastanum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BK8 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bk8 OCA], [http://pdbe.org/1bk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bk8 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/DEF1_AESHI DEF1_AESHI]] Possesses antimicrobial activity sensitive to inorganic cations. Binds specifically to the fungal plasma membrane. Has no inhibitory effect on insect gut alpha-amylase.<ref>PMID:10656585</ref> <ref>PMID:7628617</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/1bk8_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

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 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<ref>PMID:10591099</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1bk8" style="background-color:#fffaf0;"></div>

[[Category: Borremans, F A.M]]

[[Category: Fant, F]]

[[Category: Antimicrobial]]

[[Category: Plant defensin]]