1ter

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1ter.gif|left|200px]]
[[Image:1ter.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1ter |SIZE=350|CAPTION= <scene name='initialview01'>1ter</scene>
+
The line below this paragraph, containing "STRUCTURE_1ter", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1ter| PDB=1ter | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [http://www.ebi.ac.uk/pdbsum/1ter PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB]</span>
+
-
}}
+
'''SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY'''
'''SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY'''
Line 27: Line 24:
[[Category: Nelson, J W.]]
[[Category: Nelson, J W.]]
[[Category: Xu, X.]]
[[Category: Xu, X.]]
-
[[Category: toxin]]
+
[[Category: Toxin]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:51:44 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:01 2008''
+

Revision as of 06:51, 3 May 2008

Template:STRUCTURE 1ter

SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY


Overview

The solution structure of tertiapin, a 21-residue bee venom peptide, has been characterized by circular dichroism (CD), two-dimensional nuclear magnetic resonance (NMR) spectroscopy, and distance geometry. A total of 21 lowest error structures were obtained from distance geometry calculations. Superimposition of these structures shows that the backbone of tertiapin is very well defined. One type-I reverse turn from residue 4 to 7 and an alpha-helix from residue 12 to 19 exist in the structure of tertiapin. The alpha-helical region is best defined from both conformational analysis and structural superimposition. The overall three-dimensional structure of tertiapin is highly compact resulting from side chain interactions. The structural information obtained from CD and NMR are compared for both tertiapin and apamin (ref. 3), another bee venom peptide. Tertiapin and apamin have some similar secondary structure, but display different tertiary structures.

About this Structure

1TER is a Single protein structure of sequence from Apis mellifera. Full crystallographic information is available from OCA.

Reference

Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry., Xu X, Nelson JW, Proteins. 1993 Oct;17(2):124-37. PMID:8265561 Page seeded by OCA on Sat May 3 09:51:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools