1f3h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1f3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3h, resolution 2.58&Aring;" /> '''X-RAY CRYSTAL STRUC...)
Line 1: Line 1:
-
[[Image:1f3h.gif|left|200px]]<br />
+
[[Image:1f3h.gif|left|200px]]<br /><applet load="1f3h" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1f3h" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1f3h, resolution 2.58&Aring;" />
caption="1f3h, resolution 2.58&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN ANTI-APOPTOTIC PROTEIN SURVIVIN'''<br />
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN ANTI-APOPTOTIC PROTEIN SURVIVIN'''<br />
==Overview==
==Overview==
-
Survivin is a 16.5 kDa protein that is expressed during the G2/M phase of, the cell cycle and is hypothesized to inhibit a default apoptotic cascade, initiated in mitosis. This inhibitory function is coupled to survivin's, localization to the mitotic spindle. To begin to address the structural, basis of survivin's function, we report the X-ray crystal structure of a, recombinant form of full length survivin to 2.58 A resolution. Survivin, consists of two defined domains including an N-terminal Zn2+-binding BIR, domain linked to a 65 A amphipathic C-terminal alpha-helix. The crystal, structure reveals an extensive dimerization interface along a hydrophobic, surface on the BIR domain of each survivin monomer. A basic patch acting, as a sulfate/phosphate-binding module, an acidic cluster projecting off, the BIR domain, and a solvent-accessible hydrophobic surface residing on, the C-terminal amphipathic helix, are suggestive of functional, protein-protein interaction surfaces.
+
Survivin is a 16.5 kDa protein that is expressed during the G2/M phase of the cell cycle and is hypothesized to inhibit a default apoptotic cascade initiated in mitosis. This inhibitory function is coupled to survivin's localization to the mitotic spindle. To begin to address the structural basis of survivin's function, we report the X-ray crystal structure of a recombinant form of full length survivin to 2.58 A resolution. Survivin consists of two defined domains including an N-terminal Zn2+-binding BIR domain linked to a 65 A amphipathic C-terminal alpha-helix. The crystal structure reveals an extensive dimerization interface along a hydrophobic surface on the BIR domain of each survivin monomer. A basic patch acting as a sulfate/phosphate-binding module, an acidic cluster projecting off the BIR domain, and a solvent-accessible hydrophobic surface residing on the C-terminal amphipathic helix, are suggestive of functional protein-protein interaction surfaces.
==About this Structure==
==About this Structure==
-
1F3H 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 SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F3H OCA].
+
1F3H 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3H OCA].
==Reference==
==Reference==
Line 17: Line 16:
[[Category: Huang, H.]]
[[Category: Huang, H.]]
[[Category: Hunter, T.]]
[[Category: Hunter, T.]]
-
[[Category: Noel, J.P.]]
+
[[Category: Noel, J P.]]
-
[[Category: Verdecia, M.A.]]
+
[[Category: Verdecia, M A.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: ZN]]
Line 26: Line 25:
[[Category: thiol protease inhibitor]]
[[Category: thiol protease inhibitor]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:48:42 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:25 2008''

Revision as of 10:34, 21 February 2008


1f3h, resolution 2.58Å

Drag the structure with the mouse to rotate

X-RAY CRYSTAL STRUCTURE OF THE HUMAN ANTI-APOPTOTIC PROTEIN SURVIVIN

Overview

Survivin is a 16.5 kDa protein that is expressed during the G2/M phase of the cell cycle and is hypothesized to inhibit a default apoptotic cascade initiated in mitosis. This inhibitory function is coupled to survivin's localization to the mitotic spindle. To begin to address the structural basis of survivin's function, we report the X-ray crystal structure of a recombinant form of full length survivin to 2.58 A resolution. Survivin consists of two defined domains including an N-terminal Zn2+-binding BIR domain linked to a 65 A amphipathic C-terminal alpha-helix. The crystal structure reveals an extensive dimerization interface along a hydrophobic surface on the BIR domain of each survivin monomer. A basic patch acting as a sulfate/phosphate-binding module, an acidic cluster projecting off the BIR domain, and a solvent-accessible hydrophobic surface residing on the C-terminal amphipathic helix, are suggestive of functional protein-protein interaction surfaces.

About this Structure

1F3H is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement., Verdecia MA, Huang H, Dutil E, Kaiser DA, Hunter T, Noel JP, Nat Struct Biol. 2000 Jul;7(7):602-8. PMID:10876248

Page seeded by OCA on Thu Feb 21 12:34:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools