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Tachyplesin
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The aminoacid sequence of the TPI is H-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-NH₂ with <scene name='67/671725/Tachyplesin_i/1'> disulfide bonds [[Image:scheme.jpg]] | + | The aminoacid sequence of the TPI is H-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-NH₂ with <scene name='67/671725/Tachyplesin_i/1'> disulfide bonds </scene> [[Image:scheme.jpg]] between Cys³ and Cys¹⁶/Cys⁷ and Cys¹². Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. |
There are three linear derivatives: <scene name='67/671725/1ma4/1'>TPY4</scene>, TPF4 and TPA4. | There are three linear derivatives: <scene name='67/671725/1ma4/1'>TPY4</scene>, TPF4 and TPA4. | ||
Since linear tachyplesin analogues do not show preferential affinity for LPS, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | Since linear tachyplesin analogues do not show preferential affinity for LPS, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. | ||
Revision as of 11:27, 28 December 2014
Introduction
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References
- ↑ Laederach A, Andreotti AH, Fulton DB. Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives. Biochemistry. 2002 Oct 15;41(41):12359-68. PMID:12369825
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Shulamit Idzikowski, Janak Raj Joshi, Michal Harel, Alexander Berchansky, Joel L. Sussman, Angel Herraez, Jaime Prilusky
