Saposin fold revealed by the NMR structure of NK-lysin.
NK-lysin is the first representative of a family of sequence related proteins--saposins, surfactant-associated protein B, pore forming amoeba proteins, and domains of acid sphingomyelinase, acyloxyacylhydrolase and plant aspartic proteinases--for which a structure has been determined.
Liepinsh
E
E
Andersson
M
M
Ruysschaert
J M
JM
Otting
G
G
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D004220:Disulfides; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011510:Proteolipids / Q000737:chemistry*; D011663:Pulmonary Surfactants / Q000737:chemistry*; D049231:Saposins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D049128:Sphingolipid Activator Proteins; D013552:Swine
D004220:Disulfides; D006023:Glycoproteins; C093238:NK-lysin; C483345:PSAP protein, human; D011510:Proteolipids; D011663:Pulmonary Surfactants; D049231:Saposins; D049128:Sphingolipid Activator Proteins