Abstract:
:The Ala-30 and Asn-32 residues involved in the major antiparallel beta-sheet structure of human epidermal growth factor (hEGF) were substituted with various amino acid residues, and the receptor-binding affinities of the nine variant hEGFs were determined by the use of human KB cells. The Ala-30----Arg, Ala-30----His and Ala-30----Phe substitutions drastically reduced the binding affinity, suggesting that the side chain in position 30 of Ala-30 of hEGF is required to be small for the receptor binding. The Asn-32----Asp substitution significantly reduced the binding affinity, while the Asn-32----His variant could bind to the receptor as well as to the wild-type hEGF. Therefore, it seems to be important for receptor binding that the side chain in position 32 does not have a negative charge but does have an NH group. Thus, we propose that, in the ligand-receptor complex, the receptor recognizes, on one side of the antiparallel beta-sheet structure of hEGF, a wider contact area than previously suggested.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Koide H,Muto Y,Kasai H,Hoshi K,Takusari H,Kohri K,Takahashi S,Sasaki T,Tsukumo K,Miyake Tdoi
10.1016/0014-5793(92)80279-pkeywords:
subject
Has Abstract,Author List Incompletepub_date
1992-05-04 00:00:00pages
39-42issue
1eissn
0014-5793issn
1873-3468journal_volume
302pub_type
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