1ery

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ery" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ery" /> '''PHEROMONE ER-11, NMR'''<br /> ==Overview== ...)
Line 1: Line 1:
-
[[Image:1ery.gif|left|200px]]<br /><applet load="1ery" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ery.gif|left|200px]]<br /><applet load="1ery" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ery" />
caption="1ery" />
'''PHEROMONE ER-11, NMR'''<br />
'''PHEROMONE ER-11, NMR'''<br />
==Overview==
==Overview==
-
The NMR solution structure of the pheromone Er-11, a 39-residue protein, from the ciliated protozoan Euplotes raikovi, was calculated with the, distance geometry program DIANA from 449 NOE upper distance constraints, and 97 dihedral angle constraints, and the program OPAL was employed for, structure refinement by molecular mechanics energy minimization in a water, bath. For a group of 20 conformers used to characterize the solution, structure, the average of the pairwise RMS deviations from the mean, structure calculated for the backbone heavy atoms N, C alpha, and C' of, residues 2-38 was 0.30 A. The molecular architecture is dominated by an, up-down-up bundle of three short helices with residues 2-9, 12-19, and, 22-32, which is closely similar to the previously determined structures of, the homologous pheromones Er-1, Er-2, and Er-10. This finding provides, structural evidence for the capability shown by these pheromones to, compete with each other in binding reactions to their cell-surface, receptors.
+
The NMR solution structure of the pheromone Er-11, a 39-residue protein from the ciliated protozoan Euplotes raikovi, was calculated with the distance geometry program DIANA from 449 NOE upper distance constraints and 97 dihedral angle constraints, and the program OPAL was employed for structure refinement by molecular mechanics energy minimization in a water bath. For a group of 20 conformers used to characterize the solution structure, the average of the pairwise RMS deviations from the mean structure calculated for the backbone heavy atoms N, C alpha, and C' of residues 2-38 was 0.30 A. The molecular architecture is dominated by an up-down-up bundle of three short helices with residues 2-9, 12-19, and 22-32, which is closely similar to the previously determined structures of the homologous pheromones Er-1, Er-2, and Er-10. This finding provides structural evidence for the capability shown by these pheromones to compete with each other in binding reactions to their cell-surface receptors.
==About this Structure==
==About this Structure==
-
1ERY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Euplotes_raikovi Euplotes raikovi]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ERY OCA].
+
1ERY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Euplotes_raikovi Euplotes raikovi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERY OCA].
==Reference==
==Reference==
Line 21: Line 21:
[[Category: pheromone]]
[[Category: pheromone]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:15:30 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:57 2008''

Revision as of 10:30, 21 February 2008


1ery

Drag the structure with the mouse to rotate

PHEROMONE ER-11, NMR

Overview

The NMR solution structure of the pheromone Er-11, a 39-residue protein from the ciliated protozoan Euplotes raikovi, was calculated with the distance geometry program DIANA from 449 NOE upper distance constraints and 97 dihedral angle constraints, and the program OPAL was employed for structure refinement by molecular mechanics energy minimization in a water bath. For a group of 20 conformers used to characterize the solution structure, the average of the pairwise RMS deviations from the mean structure calculated for the backbone heavy atoms N, C alpha, and C' of residues 2-38 was 0.30 A. The molecular architecture is dominated by an up-down-up bundle of three short helices with residues 2-9, 12-19, and 22-32, which is closely similar to the previously determined structures of the homologous pheromones Er-1, Er-2, and Er-10. This finding provides structural evidence for the capability shown by these pheromones to compete with each other in binding reactions to their cell-surface receptors.

About this Structure

1ERY is a Single protein structure of sequence from Euplotes raikovi. Full crystallographic information is available from OCA.

Reference

The NMR solution structure of the pheromone Er-11 from the ciliated protozoan Euplotes raikovi., Luginbuhl P, Wu J, Zerbe O, Ortenzi C, Luporini P, Wuthrich K, Protein Sci. 1996 Aug;5(8):1512-22. PMID:8844842

Page seeded by OCA on Thu Feb 21 12:30:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools