[10] Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and the autosomal dominant cutis laxa.

Both components are primarily made of smaller amino acids such as glycine, valine, alanine, and proline.

[18] The feasibility of using recombinant human tropoelastin to enable elastin fiber production to improve skin flexibility in wounds and scarring has been studied.

[19][20] Elastin is made by linking together many small soluble precursor tropoelastin protein molecules (50-70 kDa), to make the final massive, insoluble, durable complex.

[21] Each tropoelastin consists of a string of 36 small domains, each weighing about 2 kDa in a random coil conformation.

The hydrophilic domains contain Lys-Ala (KA) and Lys-Pro (KP) motifs that are involved in crosslinking during the formation of mature elastin.

Tropoelastin aggregates at physiological temperature due to interactions between hydrophobic domains in a process called coacervation.

The large number of introns suggests that genetic recombination may contribute to the instability of the gene, leading to diseases such as SVAS.

[11] This article incorporates text from the United States National Library of Medicine, which is in the public domain.