2ew4
From Proteopedia
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[[Image:2ew4.gif|left|200px]] | [[Image:2ew4.gif|left|200px]] | ||
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'''Solution structure of MrIA''' | '''Solution structure of MrIA''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EW4 OCA]. | |
==Reference== | ==Reference== | ||
Solution structure of chi-conopeptide MrIA, a modulator of the human norepinephrine transporter., Nilsson KP, Lovelace ES, Caesar CE, Tynngard N, Alewood PF, Johansson HM, Sharpe IA, Lewis RJ, Daly NL, Craik DJ, Biopolymers. 2005;80(6):815-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15931669 15931669] | Solution structure of chi-conopeptide MrIA, a modulator of the human norepinephrine transporter., Nilsson KP, Lovelace ES, Caesar CE, Tynngard N, Alewood PF, Johansson HM, Sharpe IA, Lewis RJ, Daly NL, Craik DJ, Biopolymers. 2005;80(6):815-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15931669 15931669] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Alewood, P F.]] | [[Category: Alewood, P F.]] | ||
[[Category: Caesar, C E.]] | [[Category: Caesar, C E.]] | ||
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[[Category: Sharpe, I A.]] | [[Category: Sharpe, I A.]] | ||
[[Category: Tynngard, N.]] | [[Category: Tynngard, N.]] | ||
| - | [[Category: | + | [[Category: Beta hairpin]] |
| - | [[Category: | + | [[Category: Gamma turn]] |
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Revision as of 00:10, 4 May 2008
Solution structure of MrIA
Overview
The chi-conopeptides MrIA and MrIB are 13-residue peptides with two disulfide bonds that inhibit human and rat norepinephrine transporter systems and are of significant interest for the design of novel drugs involved in pain treatment. In the current study we have determined the solution structure of MrIA using NMR spectroscopy. The major element of secondary structure is a beta-hairpin with the two strands connected by an inverse gamma-turn. The residues primarily involved in activity have previously been shown to be located in the turn region (Sharpe, I. A.; Palant, E.; Schroder, C. I.; Kaye, D. M.; Adams, D. J.; Alewood, P. F.; Lewis, R. J. J Biol Chem 2003, 278, 40317-40323), which appears to be more flexible than the beta-strands based on disorder in the ensemble of calculated structures. Analogues of MrIA with N-terminal truncations indicate that the N-terminal residues play a role in defining a stable conformation and the native disulfide connectivity. In particular, noncovalent interactions between Val3 and Hyp12 are likely to be involved in maintaining a stable conformation. The N-terminus also affects activity, as a single N-terminal deletion introduced additional pharmacology at rat vas deferens, while deleting the first two amino acids reduced chi-conopeptide potency.
About this Structure
Full crystallographic information is available from OCA.
Reference
Solution structure of chi-conopeptide MrIA, a modulator of the human norepinephrine transporter., Nilsson KP, Lovelace ES, Caesar CE, Tynngard N, Alewood PF, Johansson HM, Sharpe IA, Lewis RJ, Daly NL, Craik DJ, Biopolymers. 2005;80(6):815-23. PMID:15931669 Page seeded by OCA on Sun May 4 03:10:52 2008
