1czy

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(New page: 200px<br /> <applet load="1czy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1czy, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE O...)
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<applet load="1czy" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1czy, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE'''<br />
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE'''<br />
==Overview==
==Overview==
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Many members of the tumor necrosis factor receptor (TNFR) superfamily, initiate intracellular signaling by recruiting TNFR-associated factors, (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly, diverse receptor sequences. Crystal structures of the TRAF domain of human, TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding, mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a, minor consensus motif, PxQxxD, can be defined from the structural, analysis, which encompass all known TRAF2-binding sequences. The, structural information provides a template for the further dissection of, receptor binding specificity of TRAF2 and for the understanding of the, complexity of TRAF-mediated signal transduction.
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Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. Crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a minor consensus motif, PxQxxD, can be defined from the structural analysis, which encompass all known TRAF2-binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF-mediated signal transduction.
==About this Structure==
==About this Structure==
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1CZY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CZY OCA].
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1CZY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1CZY OCA].
==Reference==
==Reference==
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[[Category: Kieff, E.]]
[[Category: Kieff, E.]]
[[Category: Kreishman, M.]]
[[Category: Kreishman, M.]]
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[[Category: Park, Y.C.]]
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[[Category: Park, Y C.]]
[[Category: Wu, H.]]
[[Category: Wu, H.]]
[[Category: Ye, H.]]
[[Category: Ye, H.]]
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[[Category: signaling protein]]
[[Category: signaling protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:27:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:27 2008''

Revision as of 10:11, 21 February 2008


1czy, resolution 2.00Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE

Overview

Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. Crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a minor consensus motif, PxQxxD, can be defined from the structural analysis, which encompass all known TRAF2-binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF-mediated signal transduction.

About this Structure

1CZY is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The structural basis for the recognition of diverse receptor sequences by TRAF2., Ye H, Park YC, Kreishman M, Kieff E, Wu H, Mol Cell. 1999 Sep;4(3):321-30. PMID:10518213

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