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| | ==Solution structure of plant defensin== | | ==Solution structure of plant defensin== |
| - | <StructureSection load='1ti5' size='340' side='right' caption='[[1ti5]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='1ti5' size='340' side='right'caption='[[1ti5]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ti5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vigna_radiata Vigna radiata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TI5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ti5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vigna_radiata Vigna radiata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TI5 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=1ti5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ti5 OCA], [http://pdbe.org/1ti5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ti5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ti5 PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ti5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ti5 OCA], [https://pdbe.org/1ti5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ti5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ti5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ti5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6T418_VIGRA Q6T418_VIGRA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Defensin|Defensin]] | + | *[[Defensin 3D structures|Defensin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Vigna radiata]] | | [[Category: Vigna radiata]] |
| - | [[Category: Chen, C S]] | + | [[Category: Chen CS]] |
| - | [[Category: Cheng, C S]] | + | [[Category: Cheng CS]] |
| - | [[Category: Hsu, M P]] | + | [[Category: Hsu MP]] |
| - | [[Category: Liu, Y J]] | + | [[Category: Liu YJ]] |
| - | [[Category: Liu, Y N]] | + | [[Category: Liu YN]] |
| - | [[Category: Lyu, P C]] | + | [[Category: Lyu PC]] |
| - | [[Category: Defensin]]
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| - | [[Category: Insecticidal activity]]
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| - | [[Category: Mung bean]]
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| - | [[Category: Plant protein]]
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| Structural highlights
Function
Q6T418_VIGRA
Publication Abstract from PubMed
Vigna radiata plant defensin 1 (VrD1) is the first reported plant defensin exhibiting insecticidal activity. We report herein the nuclear magnetic resonance solution structure of VrD1 and the implication on its insecticidal activity. The root-mean-square deviation values are 0.51 +/- 0.35 and 1.23 +/- 0.29 A for backbone and all heavy atoms, respectively. The VrD1 structure comprises a triple-stranded antiparallel beta-sheet, an alpha-helix, and a 3(10) helix stabilized by four disulfide bonds, forming a typical cysteine-stabilized alphabeta motif. Among plant defensins of known structure, VrD1 is the first to contain a 3(10) helix. Glu26 is highly conserved among defensins; VrD1 contains an arginine at this position, which may induce a shift in the orientation of Trp10, thereby promoting the formation of this 3(10) helix. Moreover, VrD1 inhibits Tenebrio molitor alpha-amylase. Alpha-amylase has an essential role in the digestion of plant starch in the insect gut, and expression of the common bean alpha-amylase inhibitor 1 in transgenic pea imparts complete resistance against bruchids. These results imply that VrD1 insecticidal activity has its basis in the inhibition of a polysaccharide hydrolase. Sequence and structural comparisons between two groups of plant defensins having different specificity toward insect alpha-amylase reveal that the loop between beta2 and beta3 is the probable binding site for the alpha-amylase. Computational docking experiments were used to study VrD1-alpha-amylase interactions, and these results provide information that may be used to improve the insecticidal activity of VrD1.
Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids.,Liu YJ, Cheng CS, Lai SM, Hsu MP, Chen CS, Lyu PC Proteins. 2006 Jun 1;63(4):777-86. PMID:16544327[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu YJ, Cheng CS, Lai SM, Hsu MP, Chen CS, Lyu PC. Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids. Proteins. 2006 Jun 1;63(4):777-86. PMID:16544327 doi:10.1002/prot.20962
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