A major G protein alpha O isoform in bovine brain is deamidated at Asn346 and Asn347, residues involved in receptor coupling.
A major G protein alpha O isoform in bovine brain is deamidated at Asn346 and Asn347, residues involved in receptor coupling.
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牛脑中主要的 G 蛋白 α O 同工型在 Asn346 和 Asn347(参与受体偶联的残基)处脱酰胺。
DOI:
10.1021/bi981642q
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发表时间:
1998
期刊:
影响因子:
--
通讯作者:
Hildebrandt,JD
中科院分区:
文献类型:
--
作者:
McIntire,WE;Schey,KL;Knapp,DR;Hildebrandt,JD
The structural differences between two major forms of the α subunit of the heterotrimeric G protein GOwere found to be due to deamidation of either of two Asn residues near the C-terminus of the proteins, in a region involved in receptor recognition. GOis the most abundant heterotrimeric G protein in mammalian brain. Two forms of the protein, GOAand GOB, are known to be generated by alternative splicing of a single GOα gene. A third isoform, αOC, represents about1/3of the αOprotein in brain and is related to αOA, from which it is thought to be generated by protein modification. Mass spectrometry and chemical derivatization of tryptic fragments of the proteins were used to localize the structural difference between αOAand αOCto a C-terminal peptide. Sequence analysis of a C-terminal chymotryptic fragment both by ion trap mass spectrometry and by Edman degradation identified Asn346 and Asn347 of αOAas alternative deamidation sites in αOC. These structural differences have immediate implications for G protein function, as they occur in a conformationally sensitive part of the protein involved in receptor recognition and activation. Since Asn347 is a conserved residue present in most G protein α subunits outside the αsfamily, these observations may have general significance for many G proteins. Deamidation may be a component of a novel process for modifying or adapting cellular responses mediated by G proteins.