Legume lectin of view of protein structure. Despite the conserved structure of the legume lectin subunit, they can adopt a wide range of quaternary structures. The reason behind this remarkable variability is probably to be found in the interaction with multivalent ligands. Legume lectin The legume lectins (or L-type lectins) are a family of sugar-binding proteins or lectins found in the seeds and, in smaller amounts, in the roots, stems, leaves and bark of plants belonging to the Fabaceae family. The exact function of the legume lectins "in vivo" is unknown but they are probably involved in the defense of plants against
Elastin glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Multiple transcript variants encoding different isoforms have been found for this gene. Elastin's soluble precursor is tropoelastin. The characterization of disorder is consistent with an entropy-driven mechanism of elastic recoil. It is concluded that conformational disorder is a constitutive feature of elastin structure and function. Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and the autosomal dominant cutis laxa. Other associated defects in elastin include Marfan syndrome, emphysema caused by α-antitrypsin deficiency, atherosclerosis, Buschke-Ollendorff syndrome, Menkes syndrome, pseudoxanthoma elasticum, and Williams