4j6q

From Proteopedia

Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form G)

Structural highlights

4j6q is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.539Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FCER2_HUMAN Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen).

Publication Abstract from PubMed

IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, FcvarepsilonRI and CD23. Crosslinking of FcvarepsilonRI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding.

Conformational plasticity at the IgE-binding site of the B-cell receptor CD23.,Dhaliwal B, Pang MO, Yuan D, Yahya N, Fabiane SM, McDonnell JM, Gould HJ, Beavil AJ, Sutton BJ Mol Immunol. 2013 Aug 6;56(4):693-697. doi: 10.1016/j.molimm.2013.07.005. PMID:23933509^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dhaliwal B, Pang MO, Yuan D, Yahya N, Fabiane SM, McDonnell JM, Gould HJ, Beavil AJ, Sutton BJ. Conformational plasticity at the IgE-binding site of the B-cell receptor CD23. Mol Immunol. 2013 Aug 6;56(4):693-697. doi: 10.1016/j.molimm.2013.07.005. PMID:23933509 doi:10.1016/j.molimm.2013.07.005