Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review

R-type Lectins

In: Essentials of Glycobiology. 2nd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009. Chapter 28.
Free Books & Documents
Review

R-type Lectins

Richard D Cummings et al.
Free Books & Documents

Excerpt

The R-type lectins are members of a superfamily of proteins, all of which contain a carbohydrate-recognition domain (CRD) that is structurally similar to the CRD in ricin. Ricin was the first lectin discovered and it is the prototypical lectin in this category. R-type lectins are present in plants, animals, and bacteria, and the plant lectins often contain a separate subunit that is a potent toxin. The structure–function relationships of this group of proteins are discussed in this chapter.

PubMed Disclaimer

References

    1. Stirpe F, Barbieri L, Battelli MG, Soria M, Lappi DA. Ribosome-inactivating proteins from plants: Present status and future prospects. Biotechnology. 1992;10:405–412. - PubMed
    1. Lord JM, Roberts LM, Robertus JD. Ricin: Structure, mode of action, and some current applications. FASEB J. 1994;8:201–208. - PubMed
    1. Clausen H, Bennett EP. A family of UDP-GalNAc: Polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation. Glycobiology. 1996;6:635–646. - PubMed
    1. Hazes B. The (QxW)3 domain: A flexible lectin scaffold. Protein Sci. 1996;5:1490–1501. - PMC - PubMed
    1. Gabius HJ. Animal lectins. Eur J Biochem. 1997;243:543–576. - PubMed

LinkOut - more resources