View source for 1kv4


==Solution structure of antibacterial peptide (Moricin)==
<StructureSection load='1kv4' size='340' side='right'caption='[[1kv4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KV4 FirstGlance]. <br>
</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=1kv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kv4 OCA], [https://pdbe.org/1kv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kv4 RCSB], [https://www.ebi.ac.uk/pdbsum/1kv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kv4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MOR1_BOMMO MOR1_BOMMO] Has antibacterial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure.<ref>PMID:8530391</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A novel antibacterial peptide, moricin, isolated from the silkworm Bombyx mori, consists of 42 amino acids. It is highly basic and the amino acid sequence has no significant similarity to those of other antibacterial peptides. The 20 structures of moricin in methanol have been determined from two-dimensional 1H-nuclear magnetic resonance spectroscopic data. The solution structure reveals an unique structure comprising of a long alpha-helix containing eight turns along nearly the full length of the peptide except for four N-terminal residues and six C-terminal residues. The electrostatic surface map shows that the N-terminal segment of the alpha-helix, residues 5-22, is an amphipathic alpha-helix with a clear separation of hydrophobic and hydrophilic faces, and that the C-terminal segment of the alpha-helix, residues 23-36, is a hydrophobic alpha-helix except for the negatively charged surface at the position of Asp30. The results suggest that the amphipathic N-terminal segment of the alpha-helix is mainly responsible for the increase in permeability of the membrane to kill the bacteria.

Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori.,Hemmi H, Ishibashi J, Hara S, Yamakawa M FEBS Lett. 2002 May 8;518(1-3):33-8. PMID:11997013<ref>PMID:11997013</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bombyx mori]]
[[Category: Large Structures]]
[[Category: Hara S]]
[[Category: Hemmi H]]
[[Category: Ishibashi J]]
[[Category: Yamakawa M]]