I want an example (with reference) for each of the following:
1. Binding of two proteins which are inactive.
2. Binding of two proteins where any one of the protein is active and other is inactive
3. Binding of two proteins where both are active
What do you mean by "active/inactive"? If a protein does form a specific complex, it has by definition at least one activity, the activity of binding its partner.
Do you mean folded/unfolded proteins?
To find two native proteins that bind to each other is trivial, look at receptor-ligand complexes . eg. insulin/insulin receptor, at antibody/antigen complexes, at complexes of enzymes with regulatory subunits. For examples of native protein binding to non-native or unfolded proteins, you best have a look at chaperones, proteins that have the function of keeping unfolded proteins in solution to allow them to fold properly. Two unfolded proteins may interact to form a complex with a defined structure, for example the leucine zipper domain of GCN4 is an unfolded peptide as a monomer, but upon interaction with its recognition motif (dimerization) forms a define leucine zipper. And this Paper describes a specific high affinity interaction of two natively unfolded domains to form a complex without a defined structure, see this paper: Borgia, A., Borgia, MB., Bugge, K., Kissling, VM., Heidarsson, PO., Fernandes, CB., Sottini, A., Soranno, A., Buholzer, KJ., Nettels, D., Kragelund, BB., Best, RB. & Schuler, B.Extreme disorder in an ultrahigh-affinity protein complex. Nature 555, 61-66 (2018). PMID: 29466338.
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