From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1f3k.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1f3k.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1f3k| PDB=1f3k | SCENE= }} | | {{STRUCTURE_1f3k| PDB=1f3k | SCENE= }} |
| | | | |
| - | '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF OMEGA-CONOTOXIN TXVII, AN L-TYPE CALCIUM CHANNEL BLOCKER'''
| + | ===THREE-DIMENSIONAL SOLUTION STRUCTURE OF OMEGA-CONOTOXIN TXVII, AN L-TYPE CALCIUM CHANNEL BLOCKER=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | We determined the three-dimensional structure of omega-conotoxin TxVII, a 26-residue peptide that is an L-type calcium channel blocker, by (1)H NMR in aqueous solution. Twenty converged structures of this peptide were obtained on the basis of 411 distance constraints obtained from nuclear Overhauser effect connectivities, 20 torsion angle constraints, and 21 constraints associated with hydrogen bonds and disulfide bonds. The root-mean-square deviations about the averaged coordinates of the backbone atoms (N, C(alpha), C, and O) and all heavy atoms were 0.50 +/- 0.09 A and 0.99 +/- 0.13 A, respectively. The structure of omega-conotoxin TxVII is composed of a triple-stranded antiparallel beta-sheet and four turns. The three disulfide bonds in omega-conotoxin TxVII form the classical cystine knot motif of toxic or inhibitory polypeptides. The overall folding of omega-conotoxin TxVII is similar to those of the N-type calcium channel blockers, omega-conotoxin GVIA and MVIIA, despite the low amino acid sequence homology among them. omega-Conotoxin TxVII exposes many hydrophobic residues to a certain surface area. In contrast, omega-conotoxin GVIA and MVIIA expose basic residues in the same way as omega-conotoxin TxVII. The channel binding site of omega-conotoxin TxVII is different from those of omega-conotoxin GVIA and MVIIA, although the overall folding of these three peptides is similar. The gathered hydrophobic residues of omega-conotoxin TxVII probably interact with the hydrophobic cluster of the alpha(1) subunit of the L-type calcium channel, which consists of 13 residues located in segments 5 and 6 in domain III and in segment 6 in domain IV.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11101291}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11101291 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11101291}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | 1F3K is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3K OCA]. | + | 1F3K is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3K OCA]. |
| | | | |
| | ==Reference== | | ==Reference== |
| Line 29: |
Line 33: |
| | [[Category: Omega-conotoxin]] | | [[Category: Omega-conotoxin]] |
| | [[Category: Triple-stranded antiparallel beta-sheet]] | | [[Category: Triple-stranded antiparallel beta-sheet]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:51:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:37:15 2008'' |
Revision as of 23:37, 30 June 2008
Template:STRUCTURE 1f3k
THREE-DIMENSIONAL SOLUTION STRUCTURE OF OMEGA-CONOTOXIN TXVII, AN L-TYPE CALCIUM CHANNEL BLOCKER
Template:ABSTRACT PUBMED 11101291
About this Structure
1F3K is a Single protein structure. Full experimental information is available from OCA.
Reference
Three-dimensional solution structure of omega-conotoxin TxVII, an L-type calcium channel blocker., Kobayashi K, Sasaki T, Sato K, Kohno T, Biochemistry. 2000 Dec 5;39(48):14761-7. PMID:11101291
Page seeded by OCA on Tue Jul 1 02:37:15 2008
