4.4 Article

Crystallization and preliminary X-ray analysis of the TRAF domain of TRAF3

Journal

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 58, Issue -, Pages 1340-1342

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444902008958

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Funding

  1. NCI NIH HHS [CA69381] Funding Source: Medline

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Tumor necrosis factor receptors (TNFR) signal events in immune responses, Ig class switching, activation of NF-kappaB or regulation of apoptosis. TNFR-associated factors (TRAFs) are adaptor proteins that connect TNFRs to downstream signaling pathways, including the NF-kappaB and c-JUN N-terminal kinase (JNK) pathways. Members of the TRAF family exist as trimers and share a conserved TRAF domain that mediates binding to the cytoplasmic domains of TNFRs. The TRAF domain from TRAF3 has been crystallized. In addition, an N-terminally truncated form of the domain has been crystallized in space group P321 with a shortened c axis and markedly improved diffraction (2.5 Angstrom resolution).

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