TRAF MOLECULES IN CELL SIGNALING

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Tumor necrosis factor receptors are cytokine receptors important in cellular signaling. CD40 is a well-characterized member of this family that is expressed on B cells and triggers immune responses, immunoglobulin class switching and activation of apoptosis. CD40 and other TNFRs such as LT? receptor rely on interactions with TRAF proteins that bind to the intracellular domain of the receptor. In previous studies, we crystallized TRAF3 bound in complex to a 20-residue fragment of CD40. TRAF3 crystals diffract to 3.2 ¿¿in the home laboratory. To study the details of binding of the CD40 and Lt?R to TRAF3, we are soaking peptides from the cytoplasmic portion of the receptors into the TRAF3 crystals. The present crystals do not diffract with a standard rotating anode source to the level of resolution required for detailed binding analyses. Therefore we plan to use synchrotron x-rays to collect data for the complexes.