Abstract:
:Estimation of a content of secondary structures from amino acid composition of IL-2 (TCGF), PDGF and transforming protein p28sis of simian sarcoma virus by means of the previously suggested nomograms (V.P. Zav'yalov and A.I. Denesyuk (1982) Immunol. Lett. 4, 7-14) allowed us to conclude that a dominant secondary structure of these proteins should be alpha-helix. Its content in PDGF and p28sis was estimated to be approximately equal to 50%, and that in IL-2 to be 50-65%. The content of beta-pleated structure in PDGF and p28sis does not exceed 10%, and that in IL-2 is found to be 20-30%. In all the proteins investigated five alpha-helical segments can be distinguished, of which one of the surfaces contains clusters of bulky hydrophobic side chains. As the number of alpha-helical segments satisfying the principles of packing into a hydrophobic core as well as the overall length of a polypeptide chain of IL-2 and PDGF coincided with those for IFNs, it was decided to arrange alpha-helices of these proteins into a globular structure by analogy with IFNs (V.P. Zav'yalov and A.I. Denesyuk (1984) Doklady Akad Nauk S.S.S.R. 275, 242-246). In consequence, identical side chains of amino acid residues were found at 9 out of 29 positions in hydrophobic cores of IFN-beta and IL-2, p28sis (PDGF), respectively. Thus the homology of hydrophobic cores of the proteins compared is greater than 30%. Probability of chance coincidences of amino acid residues in the hydrophobic cores of p28sis (PDGF) and IFN-beta is found to be 0.03, and that deduced from comparison of IL-2 and IFN-beta is 0.05.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Immunol Lettjournal_title
Immunology lettersauthors
Zav'yalov VP,Denesyuk AIdoi
10.1016/0165-2478(85)90178-6subject
Has Abstractpub_date
1985-01-01 00:00:00pages
71-9issue
2eissn
0165-2478issn
1879-0542pii
0165-2478(85)90178-6journal_volume
10pub_type
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