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• W1985758386 abstract "The crystal structure of a low-affinity human IgE receptor, CD23, is reported by Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar in this issue of Structure. This, together with a similar NMR structure by Hibbert et al., 2005Hibbert R.G. Teriete P. Grundy G.J. Beavil R.L. Reljic R. Holers V.M. Hannan J.P. Sutton B.J. Gould H.J. McDonnell J.M. J. Exp. Med. 2005; 202: 751-760Crossref PubMed Scopus (116) Google Scholar provide some insights into the function of the receptor. The crystal structure of a low-affinity human IgE receptor, CD23, is reported by Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar in this issue of Structure. This, together with a similar NMR structure by Hibbert et al., 2005Hibbert R.G. Teriete P. Grundy G.J. Beavil R.L. Reljic R. Holers V.M. Hannan J.P. Sutton B.J. Gould H.J. McDonnell J.M. J. Exp. Med. 2005; 202: 751-760Crossref PubMed Scopus (116) Google Scholar provide some insights into the function of the receptor. The low-affinity IgE receptor, CD23, is a member of the C-type lectin receptor family that also recognizes CD21 and other ligands. While IgE binding appears to be mainly mediated by protein-protein interactions, it is less clear whether CD23 recognizes CD21 in a carbohydrate-dependent manner. In particular, does CD23 functions as a bona fide calcium-dependent lectin, like the classic mannose binding protein (MBP), selectins, and DC-SIGN, or does it merely folds like a lectin, requiring neither calcium nor carbohydrate for its function, like the natural killer cell-expressed immunoreceptors CD94 and NKG2A–D? In general, the classic carbohydrate binding C-type lectins possess one to three conserved calcium binding sites and a sugar binding motif, EPN or QPD, specific for either mannose-type or galactose-type carbohydrates. In contrast, the known noncarbohydrate binding C-type lectin-like receptors appear to have lost all functional calcium sites as well as the sugar binding motif. By sequence, CD23 is most similar to DC-SIGN, which retains both the primary and the secondary Ca2+ binding sites as well as an EPN motif with preference for mannose-type sugars (Feinberg et al., 2001Feinberg H. Mitchell D.A. Drickamer K. Weiss W.I. Science. 2001; 294: 2163-2166Crossref PubMed Scopus (575) Google Scholar). At least the primary Ca2+ binding site appears conserved in CD23. The putative sugar binding motif appears crippled in human, but not animal, CD23 (Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar). Functionally, both carbohydrate-dependent and -independent binding have been prescribed for this receptor. So, if it smells like a lectin and dresses like a lectin, must it a lectin ? In this issue of Structure, Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar describe the crystal structures of the lectin domain of human CD23 in both the apo (calcium null) and the calcium bound forms, which may shed light on the function of this receptor (Figure 1). A similar structure was also determined in solution by nuclear magnetic resonance (NMR) (Hibbert et al., 2005Hibbert R.G. Teriete P. Grundy G.J. Beavil R.L. Reljic R. Holers V.M. Hannan J.P. Sutton B.J. Gould H.J. McDonnell J.M. J. Exp. Med. 2005; 202: 751-760Crossref PubMed Scopus (116) Google Scholar). In the crystal structure, the authors found that only the primary Ca2+ binding site is occupied in human CD23 and that both Loop L1, the putative secondary calcium binding loop in MBP, and L4, the primary calcium and carbohydrate binding loop in MBP, displayed large conformational changes in response to calcium binding (see Figure 2 of Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar). They then proposed that this conformational change is necessary for CD23 to bind IgE, since many of the loop residues appeared to be implicated in IgE binding, based on mutational work. This model provides a structural explanation for calcium-dependent, but carbohydrate-independent, CD23 recognition of IgE. Interestingly, an Arg residue was found to serve as a surrogate ligand at the calcium binding site in the apo-CD23 structure. An Arg was also observed to occupy a secondary calcium binding site in the structure of DC-SIGNR in the absence of carbohydrate (Snyder et al., 2005Snyder G.A. Colonna M. Sun P.D. J. Mol. Biol. 2005; 347: 979-989Crossref PubMed Scopus (34) Google Scholar). Calcium-dependent conformational changes in a C-type lectin were also observed in the structure of MBP (Ng et al., 1998Ng K.K. Park-Snyder S. Weiss W.I. Biochemistry. 1998; 37: 17965-17976Crossref PubMed Scopus (67) Google Scholar). However, the conformational changes in MBP were primarily restricted to the carbohydrate binding Loop L4, whereas both L4 and L1 displayed movement in the CD23 structure. It should be noted that Ca2+ appears to play only a limited role in CD23 recognition of IgE as the depletion of Ca2+ resulted in only a moderate decrease in IgE binding affinity (Hibbert et al., 2005Hibbert R.G. Teriete P. Grundy G.J. Beavil R.L. Reljic R. Holers V.M. Hannan J.P. Sutton B.J. Gould H.J. McDonnell J.M. J. Exp. Med. 2005; 202: 751-760Crossref PubMed Scopus (116) Google Scholar). Although the crystal structure contains no carbohydrate and thus does not address directly the requirement of carbohydrate in CD23 function, the disorder of Loop L4 in the presence of Ca2+ appears to be inconsistent with the role of the bound Ca2+ in stabilizing the carbohydrate binding conformation of the loop. In addition, Hibbert and colleagues, using NMR, observed no detectable binding between CD23 and several model carbohydrate compounds (Hibbert et al., 2005Hibbert R.G. Teriete P. Grundy G.J. Beavil R.L. Reljic R. Holers V.M. Hannan J.P. Sutton B.J. Gould H.J. McDonnell J.M. J. Exp. Med. 2005; 202: 751-760Crossref PubMed Scopus (116) Google Scholar). These results, together with the fact that the human CD23 contains a crippled “EPT” motif, make it less likely for human CD23 to function as a carbohydrate receptor, although the possibility remains for the “EPT” motif to recognize altered carbohydrates. A caveat is that CD23s from other species do contain a normal “EPN” motif (see Figure 3 of Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar), suggesting that human CD23 may be unique in its function when it comes to carbohydrate recognition. A central issue that remains to be resolved is how CD23 recognizes IgE. Both Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar and Hibbert et al., 2005Hibbert R.G. Teriete P. Grundy G.J. Beavil R.L. Reljic R. Holers V.M. Hannan J.P. Sutton B.J. Gould H.J. McDonnell J.M. J. Exp. Med. 2005; 202: 751-760Crossref PubMed Scopus (116) Google Scholar have mapped the IgE binding site, based on either mutational results or NMR titrations, to a region of CD23 distinct from the putative carbohydrate binding site, but involving portions of both Loops L1 and L4 (see Figure 7 of Wurzburg et al., 2006Wurzburg B.A. Tarchevskaya S.S. Jardetzky T.S. Structure. 2006; 14 (this issue): 1049-1058Abstract Full Text Full Text PDF PubMed Scopus (34) Google Scholar). On the IgE side, the CD23 binding region has been mapped to the Cɛ3 domain (Chretien et al., 1988Chretien I. Helm B.A. Marsh P.J. Padlan E.A. Wijdenes J. Banchereau J. J. Immunol. 1988; 141: 3128-3134PubMed Google Scholar, Ghaderi and Stanworth, 1993Ghaderi A.A. Stanworth D.R. Mol. Immunol. 1993; 30: 1655-1663Crossref PubMed Scopus (6) Google Scholar). However, the details of the atomic recognition between CD23 and IgE as well as the proposed Ca2+ function in this recognition can only be addressed when the complex structure is solved. Structural Changes in the Lectin Domain of CD23, the Low-Affinity IgE Receptor, upon Calcium BindingWurzburg et al.StructureJune, 2006In BriefCD23, the low-affinity receptor for IgE (FcɛRII), regulates IgE synthesis and also mediates IgE-dependent antigen transport and processing. CD23 is a unique Fc receptor belonging to the C-type lectin-like domain superfamily and binds IgE in an unusual, non-lectin-like manner, requiring calcium but not carbohydrate. We have solved the high-resolution crystal structures of the human CD23 lectin domain in the presence and absence of Ca2+. The crystal structures differ significantly from a previously determined NMR structure and show that calcium binding occurs at the principal binding site, but not at an auxiliary site that appears to be absent in human CD23. 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• W1985758386 title "Human CD23: Is It a Lectin in Disguise?" @default.
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