1lup

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lup.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1lup.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lup| PDB=1lup | SCENE= }}
{{STRUCTURE_1lup| PDB=1lup | SCENE= }}
-
'''Solution structure of a toxin (GsMTx2) from the tarantula, Grammostola spatulata, which inhibits mechanosensitive ion channels'''
+
===Solution structure of a toxin (GsMTx2) 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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12082099}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12082099 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12082099}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUP OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUP OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Beta-sheet]]
[[Category: Beta-sheet]]
[[Category: Inhibitor cysteine knot]]
[[Category: Inhibitor cysteine knot]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:18:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:20:06 2008''

Revision as of 19:20, 2 July 2008

Template:STRUCTURE 1lup

Solution structure of a toxin (GsMTx2) from the tarantula, Grammostola spatulata, which inhibits mechanosensitive ion channels

Template:ABSTRACT PUBMED 12082099

About this Structure

Full experimental 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 Wed Jul 2 22:20:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools