Leguminous lectin family Leguminous lectin family In molecular biology, the leguminous lectin family is a family of lectin proteins. It is one of the largest lectin families with more than 70 lectins reported in a review in 1990. Leguminous lectins consist of two or four subunits, each containing one carbohydrate-binding site. The interaction with sugars requires tightly bound calcium and manganese ions. The structural similarities of these lectins are reported by the primary structural analyses and X-ray crystallographic studies. X-ray studies have shown that the folding of the polypeptide chains in the region of the carbohydrate-binding sites is also similar, despite differences in
Myosin head although some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains, coded for by a multi-gene family. Myosin interacts with actin to convert chemical energy, in the form of ATP, to mechanical energy. The 3-D structure of the head portion of myosin has been determined and a model for actin-myosin complex has been constructed. The globular head is well conserved, and is key to contraction. Muscle contraction results from an attachment–detachment cycle between the myosin heads extending from myosin filaments and the sites on actin filaments. The myosin head first attaches to