1ca9
From Proteopedia
(New page: 200px<br /> <applet load="1ca9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ca9, resolution 2.3Å" /> '''STRUCTURE OF TNF REC...) |
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| - | [[Image:1ca9.gif|left|200px]]<br /> | + | [[Image:1ca9.gif|left|200px]]<br /><applet load="1ca9" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ca9" size=" | + | |
caption="1ca9, resolution 2.3Å" /> | caption="1ca9, resolution 2.3Å" /> | ||
'''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2'''<br /> | '''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tumour necrosis factor (TNF)-receptor-associated factors (TRAFs) form a | + | Tumour necrosis factor (TNF)-receptor-associated factors (TRAFs) form a family of cytoplasmic adapter proteins that mediate signal transduction from many members of the TNF-receptor superfamily and the interleukin-1 receptor. They are important in the regulation of cell survival and cell death. The carboxy-terminal region of TRAFs (the TRAF domain) is required for self-association and interaction with receptors. The domain contains a predicted coiled-coil region that is followed by a highly conserved TRAF-C domain. Here we report the crystal structure of the TRAF domain of human TRAF2, both alone and in complex with a peptide from TNF receptor-2 (TNF-R2). The structures reveal a trimeric self-association of the TRAF domain, which we confirm by studies in solution. The TRAF-C domain forms a new, eight-stranded antiparallel beta-sandwich structure. The TNF-R2 peptide binds to a conserved shallow surface depression on one TRAF-C domain and does not contact the other protomers of the trimer. The nature of the interaction indicates that an SXXE motif may be a TRAF2-binding consensus sequence. The trimeric structure of the TRAF domain provides an avidity-based explanation for the dependence of TRAF recruitment on the oligomerization of the receptors by their trimeric extracellular ligands. |
==About this Structure== | ==About this Structure== | ||
| - | 1CA9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1CA9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CA9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Burkitt, V.]] | [[Category: Burkitt, V.]] | ||
| - | [[Category: Park, Y | + | [[Category: Park, Y C.]] |
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
| - | [[Category: Villa, A | + | [[Category: Villa, A R.]] |
[[Category: Wu, H.]] | [[Category: Wu, H.]] | ||
[[Category: adapter protein]] | [[Category: adapter protein]] | ||
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[[Category: traf]] | [[Category: traf]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:02 2008'' |
Revision as of 10:04, 21 February 2008
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STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A PEPTIDE FROM TNF-R2
Overview
Tumour necrosis factor (TNF)-receptor-associated factors (TRAFs) form a family of cytoplasmic adapter proteins that mediate signal transduction from many members of the TNF-receptor superfamily and the interleukin-1 receptor. They are important in the regulation of cell survival and cell death. The carboxy-terminal region of TRAFs (the TRAF domain) is required for self-association and interaction with receptors. The domain contains a predicted coiled-coil region that is followed by a highly conserved TRAF-C domain. Here we report the crystal structure of the TRAF domain of human TRAF2, both alone and in complex with a peptide from TNF receptor-2 (TNF-R2). The structures reveal a trimeric self-association of the TRAF domain, which we confirm by studies in solution. The TRAF-C domain forms a new, eight-stranded antiparallel beta-sandwich structure. The TNF-R2 peptide binds to a conserved shallow surface depression on one TRAF-C domain and does not contact the other protomers of the trimer. The nature of the interaction indicates that an SXXE motif may be a TRAF2-binding consensus sequence. The trimeric structure of the TRAF domain provides an avidity-based explanation for the dependence of TRAF recruitment on the oligomerization of the receptors by their trimeric extracellular ligands.
About this Structure
1CA9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for self-association and receptor recognition of human TRAF2., Park YC, Burkitt V, Villa AR, Tong L, Wu H, Nature. 1999 Apr 8;398(6727):533-8. PMID:10206649
Page seeded by OCA on Thu Feb 21 12:04:02 2008
Categories: Homo sapiens | Protein complex | Burkitt, V. | Park, Y C. | Tong, L. | Villa, A R. | Wu, H. | Adapter protein | Cell survival | Tnf signaling | Traf
