1q4q

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(New page: 200px<br /><applet load="1q4q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q4q, resolution 2.1&Aring;" /> '''Crystal structure of ...)
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[[Image:1q4q.gif|left|200px]]<br /><applet load="1q4q" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q4q, resolution 2.1&Aring;" />
caption="1q4q, resolution 2.1&Aring;" />
'''Crystal structure of a DIAP1-Dronc complex'''<br />
'''Crystal structure of a DIAP1-Dronc complex'''<br />
==Overview==
==Overview==
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The inhibitor of apoptosis protein DIAP1 inhibits Dronc-dependent cell, death by ubiquitinating Dronc. The pro-death proteins Reaper, Hid and Grim, (RHG) promote apoptosis by antagonizing DIAP1 function. Here we report the, structural basis of Dronc recognition by DIAP1 as well as a novel, mechanism by which the RHG proteins remove DIAP1-mediated downregulation, of Dronc. Biochemical and structural analyses revealed that the second BIR, (BIR2) domain of DIAP1 recognizes a 12-residue sequence in Dronc. This, recognition is essential for DIAP1 binding to Dronc, and for targeting, Dronc for ubiquitination. Notably, the Dronc-binding surface on BIR2, coincides with that required for binding to the N termini of the RHG, proteins, which competitively eliminate DIAP1-mediated ubiquitination of, Dronc. These observations reveal the molecular mechanisms of how DIAP1, recognizes Dronc, and more importantly, how the RHG proteins remove, DIAP1-mediated ubiquitination of Dronc.
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The inhibitor of apoptosis protein DIAP1 inhibits Dronc-dependent cell death by ubiquitinating Dronc. The pro-death proteins Reaper, Hid and Grim (RHG) promote apoptosis by antagonizing DIAP1 function. Here we report the structural basis of Dronc recognition by DIAP1 as well as a novel mechanism by which the RHG proteins remove DIAP1-mediated downregulation of Dronc. Biochemical and structural analyses revealed that the second BIR (BIR2) domain of DIAP1 recognizes a 12-residue sequence in Dronc. This recognition is essential for DIAP1 binding to Dronc, and for targeting Dronc for ubiquitination. Notably, the Dronc-binding surface on BIR2 coincides with that required for binding to the N termini of the RHG proteins, which competitively eliminate DIAP1-mediated ubiquitination of Dronc. These observations reveal the molecular mechanisms of how DIAP1 recognizes Dronc, and more importantly, how the RHG proteins remove DIAP1-mediated ubiquitination of Dronc.
==About this Structure==
==About this Structure==
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1Q4Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q4Q OCA].
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1Q4Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4Q OCA].
==Reference==
==Reference==
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[[Category: ubiquitination]]
[[Category: ubiquitination]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:23:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:49 2008''

Revision as of 12:35, 21 February 2008

Image:1q4q.gif

1q4q, resolution 2.1Å

Drag the structure with the mouse to rotate

Crystal structure of a DIAP1-Dronc complex

Overview

The inhibitor of apoptosis protein DIAP1 inhibits Dronc-dependent cell death by ubiquitinating Dronc. The pro-death proteins Reaper, Hid and Grim (RHG) promote apoptosis by antagonizing DIAP1 function. Here we report the structural basis of Dronc recognition by DIAP1 as well as a novel mechanism by which the RHG proteins remove DIAP1-mediated downregulation of Dronc. Biochemical and structural analyses revealed that the second BIR (BIR2) domain of DIAP1 recognizes a 12-residue sequence in Dronc. This recognition is essential for DIAP1 binding to Dronc, and for targeting Dronc for ubiquitination. Notably, the Dronc-binding surface on BIR2 coincides with that required for binding to the N termini of the RHG proteins, which competitively eliminate DIAP1-mediated ubiquitination of Dronc. These observations reveal the molecular mechanisms of how DIAP1 recognizes Dronc, and more importantly, how the RHG proteins remove DIAP1-mediated ubiquitination of Dronc.

About this Structure

1Q4Q is a Protein complex structure of sequences from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination., Chai J, Yan N, Huh JR, Wu JW, Li W, Hay BA, Shi Y, Nat Struct Biol. 2003 Nov;10(11):892-8. Epub 2003 Sep 28. PMID:14517550

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