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This subsection of the Names and taxonomy section provides information on the name(sof the organism that is the source of the protein sequence.

AffiliationPulmonary DivisionUniversity Hospital of ZurichZurichSwitzerland.

Abnormal alpha-1 antitrypsin proteins may bind together to form a large moleculeor polymerthat cannot leave the liverThe accumulation of these polymers results in liver damageIn additionlung tissue is destroyed because not enough alpha-1 antitrypsin is available to protect against neutrophil elastasePolymers of alpha-1 antitrypsin may also contribute to excessive inflammationwhich may explain some of the other features of alpha-1 antitrypsin deficiencysuch as a skin condition called panniculitis.

Many SERPINA1 gene mutations change single protein building blocksamino acidsin alpha-1 antitrypsinwhich alters the protein’s structureThe most common mutation that causes alpha-1 antitrypsin deficiency replaces the amino acid glutamic acid with the amino acid lysine at protein position 342written as Glu342Lys or E342KThis mutation results in a version of the SERPINA1 gene called the Z allele that produces very little alpha-1 antitrypsin.

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