Untitled

Abstract

The cell membrane is a complex mixture of several classes of biomolecules but amino acids and lipids are the main constituents. For this reason we are establishing a data base of transmembrane proteins with the intent of using the data base to identify interfacial peptide sequences useful for studying protein-lipid interactions at membrane interfaces. Our present intention is to characterize transmembrane peptides and amino acids found near the membrane interface. A data base containing only signal peptides is available (G. von Heijne, Prot. Seq. Data Anal. 1:41-42, 1987).

Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R, cloned using amino acid sequence data of its soluble form, encodes both the cell surface and a soluble form of the receptor.

“…1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 NH2 Asp Ser Val Cys Pro Gin Gly Lys Tyr ILe His Pro Gin ---NH2 Gly Gln Val Glu ILe Ser Ser Cys Thr Val Asp Arg Asp Thr Val ------ILe Glu Asn COOH 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NH2 Ala Gin Val Ala Phe Thr Pro Tyr Ala Pro Glu Pro Gly Ser Thr Cys Arg Leu Arg Glu Tyr Tyr NH2 Leu Cys Ala Pro Leu Arg Lys NH2 Cys Arg Pro Gly Phe Gly Val Ala Arg NH2 Glu Tyr Tyr Asp Gln Thr Ala Gln Met Cys Cys ---NH2 Glu Tyr Tyr Asp Gin Thr Ala Gin Met Cys Cys Ser ---NH2 Ser Cys G'y Pro Ser Tyr Pro Asp ---NH2 Phe Thr Pro Tyr Ala Pro Glu Pro Gly Ser Thr Cys Arg NH2 Leu Arg Glu Tyr Tyr Asp Gln Thr Ala Gin Met Cys Cys ---NH2 Leu Arg Glu Tyr Tyr Asp Gln Thr Ala Gin Met Cys Cys ---NH2 Val Ala Phe Thr Pro Tyr Ala Pro Glu Pro Gly Ser Thr Cys Arg NH2 Cys Arg Pro Gly Phe Gly Val Ala Arg NH2 Pro Gly Trp Tyr Cys Ala Leu Ser Lys NH2 Ala Gln Val Ala Phe Thr Pro Tyr Ala Pro Glu Pro Gly Ser Thr Cys Arg NH2 lIe Cys Thr Cys Arg Pro Gly Trp Tyr Cys Ala Leu Ser ---NH2 Pro Gly Thr Glu Thr Ser Asp Val Val Cys Lys Pro Cys Ala Pro Gly Thr Phe Ser ---NH2 Pro Gly Thr Glu Thr Ser Asp Val Val Cys Lys Pro Cys Ala Pro Gly Thr Phe Ser ---NH2 Cys Arg Pro Gly Phe Gly Val Ala Arg Pro Gly Thr Glu Thr Ser Asp Val Val Cys Lys NH2 Thr Ser Asp Thr Val Cys Asp Ser Cys Glu Asp Ser Thr Tyr Thr Gln Leu Trp --- (Von Heijne, 1986) lies between the glycine and isoleucine residues designated in Figure ID as -1 and +1 respectively. The other major hydrophobic domain, located between residues 191 and 213, is flanked at both ends by several charged amino acids, characteristic of a membrane anchoring domain (Pidgeon et al, 1989). As in several other transmembrane proteins, the amino acids confining the hydrophobic domain at its COOH-terminal are basic.…”