Michael K. Hancock

TL;DR: The I- type lectins are a subset of the immunoglobulin superfamily that are capable of carbohydrate-protein interactions and there are I-type lectins recognizing sialic acids, other sugars and glycosaminoglycans.

TL;DR: Together these analyses provide strong evidence that the two Man-6-P-binding sites of the IGF-II/MPR are structurally similar to each other and to the CD-MPR and utilize a similar carbohydrate recognition mechanism.

TL;DR: These studies demonstrate the ability of domain 9 alone to fold into a high affinity carbohydrate-recognition domain whereas the domain 3 alone construct is capable of only low affinity binding toward β-glucuronidase, suggesting that residues in adjacent domains (domains 1 and/or 2) are important, either directly or indirectly, for optimal binding by domain 3.

TL;DR: The results demonstrate that the IGF-II/MPR contains two functionally distinct CRDs, which differ dramatically in their ability to recognize the distinctive modifications found on Dictyostelium discoideum lysosomal enzymes: the amino-terminal CRD binds mannose 6-sulfate and Man-6-P methyl ester with a 14-55-fold higher affinity than the carboxyl- terminal CRD.

TL;DR: To elucidate the key amino acids involved in conveying this carbohydrate specificity, site-directed mutagenesis studies were conducted on the extracytoplasmic domain of the bovine CD-MPR and four were found to be essential for ligand binding.