1jd6: Difference between revisions

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New page: left|200px<br /><applet load="1jd6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jd6, resolution 2.7Å" /> '''Crystal Structure of ...
 
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[[Image:1jd6.gif|left|200px]]<br /><applet load="1jd6" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jd6.gif|left|200px]]<br /><applet load="1jd6" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jd6, resolution 2.7&Aring;" />
caption="1jd6, resolution 2.7&Aring;" />
'''Crystal Structure of DIAP1-BIR2/Hid Complex'''<br />
'''Crystal Structure of DIAP1-BIR2/Hid Complex'''<br />


==Overview==
==Overview==
The inhibitor of apoptosis protein DIAP1 suppresses apoptosis in, Drosophila, with the second BIR domain (BIR2) playing an important role., Three proteins, Hid, Grim, and Reaper, promote apoptosis, in part by, binding to DIAP1 through their conserved N-terminal sequences. The crystal, structures of DIAP1-BIR2 by itself and in complex with the N-terminal, peptides from Hid and Grim reveal that these peptides bind a surface, groove on DIAP1, with the first four amino acids mimicking the binding of, the Smac tetrapeptide to XIAP. The next 3 residues also contribute to, binding through hydrophobic interactions. Interestingly, peptide binding, induces the formation of an additional alpha helix in DIAP1. Our study, reveals the structural conservation and diversity necessary for the, binding of IAPs by the Drosophila Hid/Grim/Reaper and the mammalian Smac, proteins.
The inhibitor of apoptosis protein DIAP1 suppresses apoptosis in Drosophila, with the second BIR domain (BIR2) playing an important role. Three proteins, Hid, Grim, and Reaper, promote apoptosis, in part by binding to DIAP1 through their conserved N-terminal sequences. The crystal structures of DIAP1-BIR2 by itself and in complex with the N-terminal peptides from Hid and Grim reveal that these peptides bind a surface groove on DIAP1, with the first four amino acids mimicking the binding of the Smac tetrapeptide to XIAP. The next 3 residues also contribute to binding through hydrophobic interactions. Interestingly, peptide binding induces the formation of an additional alpha helix in DIAP1. Our study reveals the structural conservation and diversity necessary for the binding of IAPs by the Drosophila Hid/Grim/Reaper and the mammalian Smac proteins.


==About this Structure==
==About this Structure==
1JD6 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=1JD6 OCA].  
1JD6 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=1JD6 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Chai, J.]]
[[Category: Chai, J.]]
[[Category: Cocina, A.E.]]
[[Category: Cocina, A E.]]
[[Category: Hay, B.A.]]
[[Category: Hay, B A.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
[[Category: Wu, J.W.]]
[[Category: Wu, J W.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: apoptosis]]
[[Category: apoptosis]]
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[[Category: iap]]
[[Category: iap]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:07:38 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:22 2008''

Revision as of 14:21, 21 February 2008

File:1jd6.gif


1jd6, resolution 2.7Å

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Crystal Structure of DIAP1-BIR2/Hid Complex

OverviewOverview

The inhibitor of apoptosis protein DIAP1 suppresses apoptosis in Drosophila, with the second BIR domain (BIR2) playing an important role. Three proteins, Hid, Grim, and Reaper, promote apoptosis, in part by binding to DIAP1 through their conserved N-terminal sequences. The crystal structures of DIAP1-BIR2 by itself and in complex with the N-terminal peptides from Hid and Grim reveal that these peptides bind a surface groove on DIAP1, with the first four amino acids mimicking the binding of the Smac tetrapeptide to XIAP. The next 3 residues also contribute to binding through hydrophobic interactions. Interestingly, peptide binding induces the formation of an additional alpha helix in DIAP1. Our study reveals the structural conservation and diversity necessary for the binding of IAPs by the Drosophila Hid/Grim/Reaper and the mammalian Smac proteins.

About this StructureAbout this Structure

1JD6 is a Protein complex structure of sequences from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides., Wu JW, Cocina AE, Chai J, Hay BA, Shi Y, Mol Cell. 2001 Jul;8(1):95-104. PMID:11511363

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