Figure 2 - full size

 

Figure 2.
Fig. 2. The pre-BCR CDR3-H sensing site. (A) Surface representation of the pre-BCR structure in the same orientation as shown in Fig. 1B. The VpreB unique region exits out the top of the domain, lying over the HC antigen-combining site. (B) Contact residues (29) within the SLC/HC interface zoomed into the region demarcated by the red dashed box in (A). The main chain is depicted as ribbons with contact residue side chains as sticks. SLC, red; HC, blue. Asterisk designates the interchain salt bridge between VpreB and HC. (C) At left, the CDR3-H (blue sticks) from the HC on the surface of the VpreB/ 5 segment of the SLC, showing the extent of interactions between CDR3-H and the VpreB/ 5. The contact footprint between CDR3-H and SLC is highlighted in red. To the right, a similar projection of the CDR3-H on the surface of the LC of a Fab. The contact footprint between CDR3-H and LC is highlighted in red. The CDR3-H sequence is added below both structures with the region shown in sticks highlighted (blue letters). (D) Residues demarcating the human pre-BCR CDR3-H sensing site. CDR3-H with side chains (blue), 5 (magenta), and VpreB (yellow) are shown. Pre-BCR side chains that vary between human and mice and contact CDR3-H are shown in cyan. The dashed line indicates a hydrogen bond. Below the structure, a table of amino acid differences between mice and humans in the region of the CDR3-H sensing site is appended.

The above figure is reprinted by permission from the AAAs: Science (2007, 316, 291-294) copyright 2007.