1997-2000 Publications

* = co-first author, † = corresponding author

A Novel Mechanism of TRAF Signaling Revealed by Structural and Functional Analyses of the TRADD–TRAF2 Interaction

Park Y C, Ye H, Hsia C, Segal D, Rich R L, Liou H C, Myszka D G, Wu H†. Cell (2000). PDF

TRAF proteins are major mediators for the cell activation, cell survival, and antiapoptotic functions of the TNF receptor superfamily. They can be recruited to activated TNF receptors either by direct interactions with the receptors or indirectly via the adaptor protein TRADD. We now report the structure... Read More

The structural basis for the recognition of diverse receptor sequences by TRAF2.

Ye H, Park Y C, Kreishman M, Kieff E, Wu H†. Mol Cell (1999). PDF

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,.. Read More

Structural basis for self-association and receptor recognition of human TRAF2

Park Y C, Burkitt V, Villa A R, Tong L, Wu H†. Nature (1999). PDF

Tumour necrosis factor (TNF)-receptor-associated factors (TRAFs) form a family of cytoplasmic adapter proteins that mediate signal transduction from many members of the TNF-receptor superfamily and the interleukin-1 receptor1 . They are important in the regulation of cell survival and cell death. The carboxy-terminal region of TRAFs (the TRAF domain) is required for self-association and interaction with receptors... Read More

Dimeric association and segmental variability in the crystal structure of human CD4

H Wu, P D Kwong, W A Hendrickson. Nature (1997). PDF

CD4 is a co-receptor in the cellular immune response. It increases the avidity of association between a T cell and an antigen-presenting cell by interacting with non-polymorphic portions of the complex between class II major histocompatibility complex (MHC) and T-cell receptor (TCR) molecules, and it contributes directly to signal transduction through its cytoplasmic association with the lymphocyte kinase... Read More

Other Publications (1997-2000)
* = co-first author, † = corresponding author

Ye H, Wu H. (2000). Thermodynamic characterization of the interaction between TRAF2 and tumor necrosis factor receptor peptides by isothermal titration calorimetry. Proc Natl Acad Sci U S A. 97:8961-6

Ni C Z, Welsh K, Leo E, Chiou C K, Wu H, Reed J C, Ely K R. (2000). Molecular basis for CD40 signaling mediated by TRAF3. Proc Natl Acad Sci U S A. 97:10395-9

Wu H, Park Y C, Ye H, Tong L. (1999). Structural studies of human TRAF2. in Cold Spring Harbor Symposium Quant Biol (Signaling and Gene Expression in the Immune System). 64:541-549

Bhargava G, Mui S, Pav S, Wu H, Loeber G, Tong L. (1999). Preliminary crystallographic studies of human mitochondrial NAD(P)(+)- dependent malic enzyme. J Struct Biol. 127:72-5

Xu Y, Bhargava G, Wu H, Loeber G, Tong L. (1999). Crystal structure of human mitochondrial NAD(P)+-dependent malic enzyme: a new class of oxidative decarboxylases. Structure. 41:6928-38

Lustbader J W, Lobel L, Wu H, Elliott M M. (1998). Structural and molecular studies of human chorionic gonadotropin and its receptor. Recent Prog Horm. 53:395-424