Selective loss of cysteine residues and disulphide bonds in a potato proteinase inhibitor II family.

ABSTRACT: Disulphide bonds between cysteine residues in proteins play a key role in protein folding, stability, and function. Loss of a disulphide bond is often associated with functional differentiation of the protein. The evolution of disulphide bonds is still actively debated; analysis of naturally occurring variants can promote understanding of the protein evolutionary process. One of the disulphide bond-containing protein families is the potato proteinase inhibitor II (PI-II, or Pin2, for short) superfamily, which is found in most solanaceous plants and participates in plant development, stress response, and defence. Each PI-II domain contains eight cysteine residues (8C), and two similar PI-II domains form a functional protein that has eight disulphide bonds and two non-identical reaction cent

SUBMITTER: Li XQ 

PROVIDER: S-EPMC3073943 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature