1qsc: Difference between revisions
New page: left|200px<br /> <applet load="1qsc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qsc, resolution 2.400Å" /> '''CRYSTAL STRUCTURE ... |
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[[Image:1qsc.gif|left|200px]]<br /> | [[Image:1qsc.gif|left|200px]]<br /><applet load="1qsc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1qsc, resolution 2.400Å" /> | caption="1qsc, resolution 2.400Å" /> | ||
'''CRYSTAL STRUCTURE OF THE TRAF DOMAIN OF TRAF2 IN A COMPLEX WITH A PEPTIDE FROM THE CD40 RECEPTOR'''<br /> | '''CRYSTAL STRUCTURE OF THE TRAF DOMAIN OF TRAF2 IN A COMPLEX WITH A PEPTIDE FROM THE CD40 RECEPTOR'''<br /> | ||
==Overview== | ==Overview== | ||
Tumor necrosis factor receptor superfamily members convey signals that | Tumor necrosis factor receptor superfamily members convey signals that promote diverse cellular responses. Receptor trimerization by extracellular ligands initiates signaling by recruiting members of the tumor necrosis factor receptor-associated factor (TRAF) family of adapter proteins to the receptor cytoplasmic domains. We report the 2.4-A crystal structure of a 22-kDa, receptor-binding fragment of TRAF2 complexed with a functionally defined peptide from the cytoplasmic domain of the CD40 receptor. TRAF2 forms a mushroom-shaped trimer consisting of a coiled coil and a unique beta-sandwich domain. Both domains mediate trimerization. The CD40 peptide binds in an extended conformation with every side chain in contact with a complementary groove on the rim of each TRAF monomer. The spacing between the CD40 binding sites on TRAF2 supports an elegant signaling mechanism in which trimeric, extracellular ligands preorganize the receptors to simultaneously recognize three sites on the TRAF trimer. | ||
==About this Structure== | ==About this Structure== | ||
1QSC 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 ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1QSC 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=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
[[Category: Crute, J | [[Category: Crute, J J.]] | ||
[[Category: Holton, J | [[Category: Holton, J M.]] | ||
[[Category: Kehry, M | [[Category: Kehry, M R.]] | ||
[[Category: McWhirter, S | [[Category: McWhirter, S M.]] | ||
[[Category: Pullen, S | [[Category: Pullen, S S.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
[[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 14:43:08 2008'' | ||
Revision as of 12:43, 21 February 2008
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CRYSTAL STRUCTURE OF THE TRAF DOMAIN OF TRAF2 IN A COMPLEX WITH A PEPTIDE FROM THE CD40 RECEPTOR
Overview
Tumor necrosis factor receptor superfamily members convey signals that promote diverse cellular responses. Receptor trimerization by extracellular ligands initiates signaling by recruiting members of the tumor necrosis factor receptor-associated factor (TRAF) family of adapter proteins to the receptor cytoplasmic domains. We report the 2.4-A crystal structure of a 22-kDa, receptor-binding fragment of TRAF2 complexed with a functionally defined peptide from the cytoplasmic domain of the CD40 receptor. TRAF2 forms a mushroom-shaped trimer consisting of a coiled coil and a unique beta-sandwich domain. Both domains mediate trimerization. The CD40 peptide binds in an extended conformation with every side chain in contact with a complementary groove on the rim of each TRAF monomer. The spacing between the CD40 binding sites on TRAF2 supports an elegant signaling mechanism in which trimeric, extracellular ligands preorganize the receptors to simultaneously recognize three sites on the TRAF trimer.
About this Structure
1QSC is a Single protein structure of sequence from Homo sapiens with ACE as ligand. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of CD40 recognition and signaling by human TRAF2., McWhirter SM, Pullen SS, Holton JM, Crute JJ, Kehry MR, Alber T, Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8408-13. PMID:10411888
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