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The B cell antigen receptor (BCR) plays an essential role in all phases of B cell development. Here we show that the extracellular domains of murine and human Igβ form an I-set immunoglobulin-like structure with an interchain disulfide between cysteines on their G strands. Structural and sequence analysis suggests that Igα displays a similar fold as Igβ. An Igαβ heterodimer model was generated based...
The crystal structure of a low-affinity human IgE receptor, CD23, is reported by Wurzburg et al. (2006) in this issue of Structure. This, together with a similar NMR structure by Hibbert et al. (2005) provide some insights into the function of the receptor.
Group A Streptococcus secretes cysteine proteases named Mac-1 and Mac-2 that mediate host immune evasion by targeting both IgG and Fc receptors. Here, we report the crystal structures of Mac-1 and its catalytically inactive C94A mutant in two different crystal forms. Despite the lack of sequence homology, Mac-1 adopts the canonical papain fold. Alanine mutations at the active site confirmed the critical...
Triggering receptors expressed on myeloid cells (TREM) are a family of recently discovered receptors that play important roles in innate immune responses, such as to activate inflammatory responses and to contribute to septic shock in response to microbial-mediated infections. To date, two TREM receptors in human and several homologs in mice have been identified. We report the 2.6 A resolution crystal...
The crystal structure of BMP7 in complex with the type II activin receptor shows a different receptor binding site on the ligand compared to that observed in the TGF-β3 and receptor complex. The result highlights the potential diversity in ligand recognition among members of the TGF-β superfamily.
Transforming growth factor β (TGF-β) is involved in a wide range of biological functions including development, carcinogenesis, and immune regulation. Here we report the 1.1 A resolution crystal structure of human TGF-β type II receptor ectodomain (TBRII). The overall structure of TBRII is similar to that of activin type II receptor ectodomain (ActRII) and bone morphogenic protein receptor type IA...
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