2qra: Difference between revisions

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==Overview==

X-linked inhibitor of apoptosis (XIAP) is a potent negative regulator of, apoptosis. It also plays a role in BMP signaling, TGF-beta signaling, and, copper homeostasis. Previous structural studies have shown that the, baculoviral IAP repeat (BIR2 and BIR3) domains of XIAP interact with the, IAP-binding-motifs (IBM) in several apoptosis proteins such as Smac and, caspase-9 via the conserved IBM-binding groove. Here, we report the, crystal structure in two crystal forms of the BIR1 domain of XIAP, which, does not possess this IBM-binding groove and cannot interact with Smac or, caspase-9. Instead, the BIR1 domain forms a conserved dimer through the, region corresponding to the IBM-binding groove. Structural and sequence, analyses suggest that this dimerization of BIR1 in XIAP may be conserved, in other IAP family members such as cIAP1 and cIAP2 and may be important, for the action of XIAP in TGF-beta and BMP signaling and the action of, cIAP1 and cIAP2 in TNF receptor signaling.

X-linked inhibitor of apoptosis (XIAP) is a potent negative regulator of apoptosis. It also plays a role in BMP signaling, TGF-beta signaling, and copper homeostasis. Previous structural studies have shown that the baculoviral IAP repeat (BIR2 and BIR3) domains of XIAP interact with the IAP-binding-motifs (IBM) in several apoptosis proteins such as Smac and caspase-9 via the conserved IBM-binding groove. Here, we report the crystal structure in two crystal forms of the BIR1 domain of XIAP, which does not possess this IBM-binding groove and cannot interact with Smac or caspase-9. Instead, the BIR1 domain forms a conserved dimer through the region corresponding to the IBM-binding groove. Structural and sequence analyses suggest that this dimerization of BIR1 in XIAP may be conserved in other IAP family members such as cIAP1 and cIAP2 and may be important for the action of XIAP in TGF-beta and BMP signaling and the action of cIAP1 and cIAP2 in TNF receptor signaling.

==Disease==

Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300079 300079]]

==About this Structure==

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==Reference==

Crystal ~~Structure~~ of the BIR1 ~~Domain~~ of XIAP in ~~Two Crystal Forms~~., Lin SC, Huang Y, Lo YC, Lu M, Wu H, J Mol Biol. 2007 Sep 28;372(4):847-54. Epub 2007 Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17698078 17698078]

Crystal structure of the BIR1 domain of XIAP in two crystal forms., Lin SC, Huang Y, Lo YC, Lu M, Wu H, J Mol Biol. 2007 Sep 28;372(4):847-54. Epub 2007 Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17698078 17698078]

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Lin, S.C.]]

[[Category: Lin, S C.]]

[[Category: EOH]]

[[Category: ZN]]

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[[Category: zinc binding]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-X-linked inhibitor of apoptosis (XIAP) is a potent negative regulator of, apoptosis. It also plays a role in BMP signaling, TGF-beta signaling, and, copper homeostasis. Previous structural studies have shown that the, baculoviral IAP repeat (BIR2 and BIR3) domains of XIAP interact with the, IAP-binding-motifs (IBM) in several apoptosis proteins such as Smac and, caspase-9 via the conserved IBM-binding groove. Here, we report the, crystal structure in two crystal forms of the BIR1 domain of XIAP, which, does not possess this IBM-binding groove and cannot interact with Smac or, caspase-9. Instead, the BIR1 domain forms a conserved dimer through the, region corresponding to the IBM-binding groove. Structural and sequence, analyses suggest that this dimerization of BIR1 in XIAP may be conserved, in other IAP family members such as cIAP1 and cIAP2 and may be important, for the action of XIAP in TGF-beta and BMP signaling and the action of, cIAP1 and cIAP2 in TNF receptor signaling.
+X-linked inhibitor of apoptosis (XIAP) is a potent negative regulator of apoptosis. It also plays a role in BMP signaling, TGF-beta signaling, and copper homeostasis. Previous structural studies have shown that the baculoviral IAP repeat (BIR2 and BIR3) domains of XIAP interact with the IAP-binding-motifs (IBM) in several apoptosis proteins such as Smac and caspase-9 via the conserved IBM-binding groove. Here, we report the crystal structure in two crystal forms of the BIR1 domain of XIAP, which does not possess this IBM-binding groove and cannot interact with Smac or caspase-9. Instead, the BIR1 domain forms a conserved dimer through the region corresponding to the IBM-binding groove. Structural and sequence analyses suggest that this dimerization of BIR1 in XIAP may be conserved in other IAP family members such as cIAP1 and cIAP2 and may be important for the action of XIAP in TGF-beta and BMP signaling and the action of cIAP1 and cIAP2 in TNF receptor signaling.
+==Disease==
+Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300079 300079]]
 ==About this Structure==
@@ Line 10: / Line 13: @@
 ==Reference==
-Crystal Structure of the BIR1 Domain of XIAP in Two Crystal Forms., Lin SC, Huang Y, Lo YC, Lu M, Wu H, J Mol Biol. 2007 Sep 28;372(4):847-54. Epub 2007 Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17698078 17698078]
+Crystal structure of the BIR1 domain of XIAP in two crystal forms., Lin SC, Huang Y, Lo YC, Lu M, Wu H, J Mol Biol. 2007 Sep 28;372(4):847-54. Epub 2007 Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17698078 17698078]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Lin, S.C.]]
+[[Category: Lin, S C.]]
 [[Category: EOH]]
 [[Category: ZN]]
@@ Line 20: / Line 23: @@
 [[Category: zinc binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:06:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:39 2008''