1l0a: Difference between revisions

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==Overview==
==Overview==
TRAFs (tumor necrosis factor receptor [TNFR]-associated factors) bind to, the cytoplasmic portion of liganded TNFRs and stimulate activation of, NF-kappaB or JNK pathways. A modulator of TRAF signaling, TANK, serves as, either an enhancer or an inhibitor of TRAF-mediated signaling pathways., The crystal structure of a region of TANK bound to TRAF3 has been, determined and compared to a similar CD40/TRAF3 complex. TANK and CD40, bind to the same crevice on TRAF3. The recognition motif PxQxT is, presented in a boomerang-like structure in TANK that is markedly different, from the hairpin loop that forms in CD40 upon binding to TRAF3. Critical, TANK contact residues were confirmed by mutagenesis to be required for, binding to TRAF3 or TRAF2. Binding affinity, measured by isothermal, titration calorimetry and competition assays, demonstrated that TANK, competes with CD40 for the TRAF binding site.
TRAFs (tumor necrosis factor receptor [TNFR]-associated factors) bind to the cytoplasmic portion of liganded TNFRs and stimulate activation of NF-kappaB or JNK pathways. A modulator of TRAF signaling, TANK, serves as either an enhancer or an inhibitor of TRAF-mediated signaling pathways. The crystal structure of a region of TANK bound to TRAF3 has been determined and compared to a similar CD40/TRAF3 complex. TANK and CD40 bind to the same crevice on TRAF3. The recognition motif PxQxT is presented in a boomerang-like structure in TANK that is markedly different from the hairpin loop that forms in CD40 upon binding to TRAF3. Critical TANK contact residues were confirmed by mutagenesis to be required for binding to TRAF3 or TRAF2. Binding affinity, measured by isothermal titration calorimetry and competition assays, demonstrated that TANK competes with CD40 for the TRAF binding site.


==About this Structure==
==About this Structure==
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[[Category: Cabezas, E.]]
[[Category: Cabezas, E.]]
[[Category: Cheng, G.]]
[[Category: Cheng, G.]]
[[Category: Ely, K.R.]]
[[Category: Ely, K R.]]
[[Category: Havert, M.L.]]
[[Category: Havert, M L.]]
[[Category: He, J.]]
[[Category: He, J.]]
[[Category: Kaiser, D.]]
[[Category: Kaiser, D.]]
[[Category: Li, C.]]
[[Category: Li, C.]]
[[Category: Ni, C.Z.]]
[[Category: Ni, C Z.]]
[[Category: Reed, J.C.]]
[[Category: Reed, J C.]]
[[Category: Satterthwait, A.C.]]
[[Category: Satterthwait, A C.]]
[[Category: cd40]]
[[Category: cd40]]
[[Category: nf-kb signaling]]
[[Category: nf-kb signaling]]
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[[Category: traf3]]
[[Category: traf3]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:53 2008''

Revision as of 11:39, 21 February 2008

File:1l0a.jpg


1l0a, resolution 2.9Å

Drag the structure with the mouse to rotate

DOWNSTREAM REGULATOR TANK BINDS TO THE CD40 RECOGNITION SITE ON TRAF3

Overview

TRAFs (tumor necrosis factor receptor [TNFR]-associated factors) bind to the cytoplasmic portion of liganded TNFRs and stimulate activation of NF-kappaB or JNK pathways. A modulator of TRAF signaling, TANK, serves as either an enhancer or an inhibitor of TRAF-mediated signaling pathways. The crystal structure of a region of TANK bound to TRAF3 has been determined and compared to a similar CD40/TRAF3 complex. TANK and CD40 bind to the same crevice on TRAF3. The recognition motif PxQxT is presented in a boomerang-like structure in TANK that is markedly different from the hairpin loop that forms in CD40 upon binding to TRAF3. Critical TANK contact residues were confirmed by mutagenesis to be required for binding to TRAF3 or TRAF2. Binding affinity, measured by isothermal titration calorimetry and competition assays, demonstrated that TANK competes with CD40 for the TRAF binding site.

About this Structure

1L0A is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Downstream regulator TANK binds to the CD40 recognition site on TRAF3., Li C, Ni CZ, Havert ML, Cabezas E, He J, Kaiser D, Reed JC, Satterthwait AC, Cheng G, Ely KR, Structure. 2002 Mar;10(3):403-11. PMID:12005438

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