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<StructureSection load='' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>
<StructureSection load='' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>
== Introduction ==
== Introduction ==
Tachyplesin I (TP-I) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth  of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].
'''Tachyplesin I, II and III''' are [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth  of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].
The antimicrobial activity of the polypeptide is contributed by electrostatic interaction between the negatively charged membrane of bacteria and fungi to positively charged part of <scene name='67/671725/Cationic_peptide_tpi/3'> TP-I </scene> <ref name=Laederach>PMID:12369825</ref> (see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Charge_Cationic}} amino acids).
The antimicrobial activity of the polypeptide is contributed by electrostatic interaction between the negatively charged membrane of bacteria and fungi to positively charged part of <scene name='67/671725/Cationic_peptide_tpi/3'> TP-I </scene> <ref name=Laederach>PMID:12369825</ref> (see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Charge_Cationic}} amino acids).
Specifically, TP-I shows high affinity for negatively charged [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects.  
Specifically, TP-I shows high affinity for negatively charged [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects.  
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[http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water  surrounding</scene>  to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>.
[http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water  surrounding</scene>  to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>.


== Derivatives or Analogue ==
== Derivatives or Analogue ==
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==3D structure of tachyplesin==
==3D structure of tachyplesin==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|


[[1ma2]], [[1ma5]], [[1wo0]], [[1wo1]], [[2mdb]], [[2rtv]] – TacI peptide residues 24-40  – Japanese horseshoe crab - NMR<br />
*Tachyplesin I 
[[1ma4]], [[1ma6]] – TacI peptide residues 24-40 (mutant) - NMR<br />
[[2lm8]] – TacI peptide residues 1-13 (mutant) - NMR<br />


**[[1ma2]], [[1ma5]], [[1wo0]], [[1wo1]], [[2mdb]], [[2rtv]], [[6pin]] – TtTacI peptide residues 24-40  – Tachypleus tridentatus -  - NMR<br />
**[[1ma4]], [[1ma6]] – TtTacI peptide residues 24-40 (mutant) - NMR<br />
**[[2lm8]] – TacI peptide residues 1-13 (mutant) - NMR<br />


*Tachyplesin II 
**[[6pio]] – TtTacII peptide residues 24-40  - NMR<br />
**[[6pi2]] – TacII peptide residues 24-40  - Limulus polyphemus - NMR<br />
*Tachyplesin III 
**[[6pip]], [[6pi3]] – TacIII + peptide residues 24-40  - Tachypleus gigas - NMR<br />
}}


== Quiz ==
== Quiz ==
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</Quiz>
</Quiz>
</StructureSection>


== References ==
== References ==
<references/>
<references/>
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]
[[Category:Pages with quizzes]]
[[Category:Pages with quizzes]]

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Janak Raj Joshi, Shulamit Idzikowski, Michal Harel, Alexander Berchansky, Joel L. Sussman, Angel Herraez, Jaime Prilusky
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