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Coefficient of functional divergence

Our results indicated that all the functional sites of AVP-R were highly conserved, which makes it a potential drug target. However, most mutations (242/268) were found in the binding site and in the response regulator (RR) region which is responsible for response of the protein to the signal. According to Csa–[@ref24], 53% of drug-resistance mutation sites in AVP-R are located in the catalytic domain. From our results, it was clear that the overall sequence alignment of AVP-R is more conserved than the catalytic domain. Furthermore, among the catalytic domains, the active site region was the least conserved, which might be responsible for the activity of AVP-R.

Experimental approaches to detect the structure of AVP-R {#sec2-14}

It was very interesting to us to develop a method for the crystallization of AVP-R. The sequence alignment of AVP-R with the homologous proteins showed that no significant sequence similarity to known proteins. Therefore, random mutagenesis of AVP-R might have been the best method. However, it took a lot of time and effort to express and purify AVP-R. We also suggested that the development of the specific antibodies directed to the N-terminal region of AVP-R might be more promising. In fact, we could not find any non-specific antibodies to the recombinant AVP-R.

Conclusion {#sec1-4}

The overall structure of AVP-R and its catalytic domain is different from its orthologous proteins. There were no significant homology with the protein structures reported in the PDB. The binding site and the potential binding site for AVP are different from all of the homologous proteins. In addition, the sites of mutations found in the protein were also different from those reported in literature for any protein. The efficiency of the design of AVP-R was low, and further research on this drug target should be supported in terms of structure and validation. The method proposed to design this drug target was able to design a human AVP-R whose sequence was different from the one in the r


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