Our studies provide a structural platform for understanding B cell signalling and designing rational therapies against BCR-mediated diseases. B cells can recognize structurally diverse...

The B cell receptor (BCR) initiates immune responses through antigen recognition. We report a 3.3-angstrom cryo–electron microscopy structure of human immunoglobulin M (IgM)–BCR in the resting …

The chapter provides an in-depth analysis of the B cell receptor (BCR), a critical immunoglobulin molecule on B lymphocytes that significantly influences B cell survival, development, and activation. …

BCR consists of two immunoglobulin heavy chains (Igα and Igβ) and two light chains (mIg), forming a heterodimer complex. Among them, mIg is the key part of antigen recognition, which can be divided …

In this chapter, we describe the basic structure of the BCR in light of recent cryo-electron microscopy (cryo-EM) studies and discuss the regulation, antigen-sensing and intracellular signalling …

These findings explain the molecular principles underlying BCR assembly and provide opportunities for structure-guided rational engineering of BCRs for the treatment of hematological and autoimmune …

The B cell receptor (BCR) is a molecular complex displayed on the B cell surface that allows it to recognize foreign invaders. Each B cell expresses millions of identical BCRs, and each B cell is …

This structure contains 14 glycosylation sites on the IgM-BCR ectodomains and reveals three potential surface binding sites. Our work reveals the organizational principles of the BCR and may facilitate …

Each B cell occupies a unique B cell receptor (BCR), and all BCRs throughout our body form “BCR repertoire”.

We now show that the ligand-binding membrane immunoglobulin (mIg) TM domains in the B cell receptor (BCR) form a core structure that is strikingly similar to that of the TCR and plays a crucial …