Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus
β Scribed by Lieven Buts; Minh-Hoa Dao-Thi; Remy Loris; Lode Wyns; Marilynn Etzler; Thomas Hamelryck
- Book ID
- 115631016
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 426 KB
- Volume
- 309
- Category
- Article
- ISSN
- 0022-2836
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π SIMILAR VOLUMES
Legume lectins constitute a family of proteins in which small alterations arising from sequence variations in essentially the same tertiary structure lead to large changes in quaternary association. All of them are dimers or tetramers made up of dimers. Dimerization involves side-by-side or back-to-
## Abstract During the course of characterization of low molecular weight proteins in cartilage, we have isolated a protein from reef shark __(Carcharhinus springeri)__ cartilage that bears a striking resemblance to the tetranectin monomer originally described by Clemmensen et al. (1986, __Eur. J.