The carbohydrate-recognition domain (CRD) of Dectin-2 exhibited cation-dependent mannose/fucose-like lectin activity, with an IC(50) for mannose of approximately 20 mM compared to an IC(50) of 1.5 mM for the macrophage mannose receptor when assayed by similar methodology. The extracellular ...
The expressed rCRD-N, which had a T7·Tag fused to the N-terminus and a histidine-rich peptide chain fused to the C-terminus, carried residues 22–147 of the H. cunea lectin, corresponding to the CRD-N domain. The rCRD-C contains a T7·Tag in the N-terminus and the CRD-C ...
2) carbohydrate recognition domain 糖识别域 1. Prokaryotic expression of Balb/C mouse MBL-A carbohydrate recognition domain Balb/C小鼠甘露聚糖结合凝集素-A糖识别域的原核表达 更多例句>> 3) peptidoglycan recognition proteins 肽聚糖识别蛋白 1. Peptidoglycan recognition proteins (PGRPs) are pattern ...
We have determined the crystal structure of the carbohydrate recognition domain (CRD) of p58, the rat homologue of human ERGIC-53, to 1.46 resolution. The fold and ligand binding site are most similar to those of leguminous lectins. The structure also resembles that of the CRD of the ER ...
We have previously reported that the carbohydrate recognition domain of SP-D plays an essential role in lipid binding. However, it is unclear how the carbohydrate binding property of SP-D contributes to the lipid binding. To clarify the relationship between the lectin property and the lipid ...
CRD that comprises approximately 130 amino acids. The only member of the chimera type, galectin-3, has anN-terminal short peptide motif, a flexible collagen-like Gly/Pro/Tyr-rich domain, which induces self-oligomerization1and a CRD at itsC-terminus. The tandem-repeat galectins, of which ...
We found that the N-terminal CRD of Hco-gal-m (MNh) and the C-terminal CRD (MCh) could bind to goat peripheral blood mononuclear cells by distinct receptors: transmembrane protein 63A (TMEM63A) was a binding receptor of MNh, while transmembrane protein 147 (TMEM147) was a binding ...
Selectins are a family of adhesion molecules with a well-defined domain structure comprised of a lectin or carbohydrate-recognition domain (CRD), an epidermal growth factor (EGF)-like motif, and a variable number of consensus repeats (CRs). While it is clear from various lines of evidence ...
The carbohydrate-recognition domain (CRD), which is localized at the opposite of the receptor-binding domain, makes these molecules bi-functional. The expression of the biological activity of the cytokine relies on its carbohydrate-binding activity, which allows the association of the cytokine ...
We have determined the crystal structure of CRD-4. Although the basic C-type lectin fold is preserved, a loop extends away from the core of the domain to form a domain-swapped dimer in the crystal. Of the two Ca(2+) sites, only the principal site known to mediate carbohydrate binding ...