1tyk
From Proteopedia
(New page: 200px<br /><applet load="1tyk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tyk" /> '''SOLUTION STRUCTURE OF A TOXIN FROM THE TARAN...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1tyk.jpg|left|200px]]<br /><applet load="1tyk" size=" | + | [[Image:1tyk.jpg|left|200px]]<br /><applet load="1tyk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tyk" /> | caption="1tyk" /> | ||
'''SOLUTION STRUCTURE OF A TOXIN FROM THE TARANTULA, GRAMMOSTOLA SPATULATA, WHICH INHIBITS MECHANOSENSITIVE ION CHANNELS'''<br /> | '''SOLUTION STRUCTURE OF A TOXIN FROM THE TARANTULA, GRAMMOSTOLA SPATULATA, WHICH INHIBITS MECHANOSENSITIVE ION CHANNELS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mechanosensitive channels (MSCs) play key roles in sensory processing and | + | Mechanosensitive channels (MSCs) play key roles in sensory processing and have been implicated as primary transducers for a variety of cellular responses ranging from osmosensing to gene expression. This paper presents the first structures of any kind known to interact specifically with MSCs. GsMTx-4 and GsMtx-2 are inhibitor cysteine knot peptides isolated from venom of the tarantula, Grammostola spatulata (Suchyna, T. M., Johnson, J. H., Hamer, K., Leykam, J. F., Gage, D. A., Clemo, H. F., Baumgarten, C. M., and Sachs, F. (2000) J. Gen. Physiol. 115, 583-598). Inhibition of cationic MSCs by the higher affinity GsMtx-4 (K(D) approximately 500 nm) reduced cell size in swollen and hypertrophic heart cells, swelling-activated currents in astrocytes, and stretch-induced arrhythmias in the heart. Despite the relatively low affinity, no cross-reactivity has been found with other channels. Using two-dimensional NMR spectroscopy, we determined the solution structure of GsMTx-4 and a lower affinity (GsMTx-2; K(D) approximately 6 microm) peptide from the same venom. The dominant feature of the two structures is a hydrophobic patch, utilizing most of the aromatic residues and surrounded with charged residues. The spatial arrangement of charged residues that are unique to GsMTx-4 and GsMTx-2 may underlie the selectivity of these peptides. |
==About this Structure== | ==About this Structure== | ||
| - | 1TYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Grammostola_rosea Grammostola rosea]. This structure | + | 1TYK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Grammostola_rosea Grammostola rosea]. This structure supersedes the now removed PDB entry 1LQR. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYK OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Gottlieb, P.]] | [[Category: Gottlieb, P.]] | ||
[[Category: Mcfeeters, R.]] | [[Category: Mcfeeters, R.]] | ||
| - | [[Category: Oswald, R | + | [[Category: Oswald, R E.]] |
[[Category: Sachs, F.]] | [[Category: Sachs, F.]] | ||
| - | [[Category: Suchyna, T | + | [[Category: Suchyna, T M.]] |
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
[[Category: cysteine knot]] | [[Category: cysteine knot]] | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:44 2008'' |
Revision as of 13:18, 21 February 2008
|
SOLUTION STRUCTURE OF A TOXIN FROM THE TARANTULA, GRAMMOSTOLA SPATULATA, WHICH INHIBITS MECHANOSENSITIVE ION CHANNELS
Overview
Mechanosensitive channels (MSCs) play key roles in sensory processing and have been implicated as primary transducers for a variety of cellular responses ranging from osmosensing to gene expression. This paper presents the first structures of any kind known to interact specifically with MSCs. GsMTx-4 and GsMtx-2 are inhibitor cysteine knot peptides isolated from venom of the tarantula, Grammostola spatulata (Suchyna, T. M., Johnson, J. H., Hamer, K., Leykam, J. F., Gage, D. A., Clemo, H. F., Baumgarten, C. M., and Sachs, F. (2000) J. Gen. Physiol. 115, 583-598). Inhibition of cationic MSCs by the higher affinity GsMtx-4 (K(D) approximately 500 nm) reduced cell size in swollen and hypertrophic heart cells, swelling-activated currents in astrocytes, and stretch-induced arrhythmias in the heart. Despite the relatively low affinity, no cross-reactivity has been found with other channels. Using two-dimensional NMR spectroscopy, we determined the solution structure of GsMTx-4 and a lower affinity (GsMTx-2; K(D) approximately 6 microm) peptide from the same venom. The dominant feature of the two structures is a hydrophobic patch, utilizing most of the aromatic residues and surrounded with charged residues. The spatial arrangement of charged residues that are unique to GsMTx-4 and GsMTx-2 may underlie the selectivity of these peptides.
About this Structure
1TYK is a Single protein structure of sequence from Grammostola rosea. This structure supersedes the now removed PDB entry 1LQR. Full crystallographic information is available from OCA.
Reference
Solution structure of peptide toxins that block mechanosensitive ion channels., Oswald RE, Suchyna TM, McFeeters R, Gottlieb P, Sachs F, J Biol Chem. 2002 Sep 13;277(37):34443-50. Epub 2002 Jun 24. PMID:12082099
Page seeded by OCA on Thu Feb 21 15:18:44 2008
