1e31

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1e31" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e31, resolution 2.71&Aring;" /> '''SURVIVIN DIMER H. S...)
Line 1: Line 1:
-
[[Image:1e31.gif|left|200px]]<br />
+
[[Image:1e31.gif|left|200px]]<br /><applet load="1e31" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1e31" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1e31, resolution 2.71&Aring;" />
caption="1e31, resolution 2.71&Aring;" />
'''SURVIVIN DIMER H. SAPIENS'''<br />
'''SURVIVIN DIMER H. SAPIENS'''<br />
==Overview==
==Overview==
-
Survivin is a mitotic spindle-associated protein involved in linking, mitotic spindle function to activation of apoptosis in mammalian cells., The structure of the full-length human survivin has been determined by, X-ray crystallography to 2.7 A. Strikingly, the structure forms a very, unusual bow tie-shaped dimer. It does not dimerize through a C-terminal, coiled-coil, contrary to sequence analysis prediction. The C-terminal, helices contain hydrophobic clusters with the potential for, protein-protein interactions. The unusual shape and dimensions of survivin, suggest it serves an adaptor function through its alpha-helical, extensions.
+
Survivin is a mitotic spindle-associated protein involved in linking mitotic spindle function to activation of apoptosis in mammalian cells. The structure of the full-length human survivin has been determined by X-ray crystallography to 2.7 A. Strikingly, the structure forms a very unusual bow tie-shaped dimer. It does not dimerize through a C-terminal coiled-coil, contrary to sequence analysis prediction. The C-terminal helices contain hydrophobic clusters with the potential for protein-protein interactions. The unusual shape and dimensions of survivin suggest it serves an adaptor function through its alpha-helical extensions.
==About this Structure==
==About this Structure==
-
1E31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and CO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E31 OCA].
+
1E31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E31 OCA].
==Reference==
==Reference==
Line 24: Line 23:
[[Category: zinc finger]]
[[Category: zinc finger]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:39:11 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:14 2008''

Revision as of 10:23, 21 February 2008


1e31, resolution 2.71Å

Drag the structure with the mouse to rotate

SURVIVIN DIMER H. SAPIENS

Overview

Survivin is a mitotic spindle-associated protein involved in linking mitotic spindle function to activation of apoptosis in mammalian cells. The structure of the full-length human survivin has been determined by X-ray crystallography to 2.7 A. Strikingly, the structure forms a very unusual bow tie-shaped dimer. It does not dimerize through a C-terminal coiled-coil, contrary to sequence analysis prediction. The C-terminal helices contain hydrophobic clusters with the potential for protein-protein interactions. The unusual shape and dimensions of survivin suggest it serves an adaptor function through its alpha-helical extensions.

About this Structure

1E31 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions., Chantalat L, Skoufias DA, Kleman JP, Jung B, Dideberg O, Margolis RL, Mol Cell. 2000 Jul;6(1):183-9. PMID:10949039

Page seeded by OCA on Thu Feb 21 12:23:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools