Mannan-binding lectin Mannan-binding lectin Mannose-binding lectin (MBL), also called mannose-binding protein or mannan-binding protein (MBP), is a lectin that is instrumental in innate immunity via the lectin pathway. MBL has an oligomeric structure (400-700 kDa), built of subunits that contain three presumably identical peptide chains of about 30 kDa each. Although MBL can form several oligomeric forms, there are indications that dimers and trimers are not biologically active and at least a tetramer form is needed for activation of complement. Human MBL2 gene is located on chromosome 10q11.2-q21. Mice have two homologous genes, but in human the first of them was lost.
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