Summary

     It includes studying  the features of  CRP belong to pentraxin family of the genetic site 1q23.2  by using bioinformatics methods for individuals with different cancers and poisoning thyroid gland disease,  and compared with standard samples.

    In present study, whole blood and serum were isolated from  200 individuals distributed to two group:

1. One hundred and fifty patients, with different cancer types and poisoning thyroid gland from differential provinces, of both sexes and different age groups.
2. Fifty apparently healthy volunteers.

     The results of the qualitative test demonstrated the potential of the use of CRP protein as a marker of the incidence of  poisoning thyroid gland disease  and this is evidence that inflammatory plays an important role in the dysfunction of thyroid gland, and  unable of using CRP as a marker of the incidence of various cancers. The results of HPLC analysis showed that patients who had a protein in serum had a higher than normal rate, while the level of CRP in patients with cancer more than patients with poisoning  thyroid gland disease. The extracted DNA was used to study the genetic variance of CRP gene. The results of BLAST  program that used for detection the mutations in CRP gene for the sequence of the studied samples, appearance about 107 mutation in five patients with cancer and one patient with poising thyroid gland disease. Missens mutations recorded about 52.33% , this consider the highest percentage of other mutations, while the deletion mutation recorded about 32.71% , insertion mutation recorded13.1%  and frame-shift reading mutations recorded about 1.86%. The point mutation was identified at site 159714441 for the first Exon of the CRP gene that had the same effect. Thymine replacement was replaced by the adenin. This mutation was shown in five patients  with head, bone, kidney, lung and breast cancer. . This mutation was recorded with symbols LC276934, LC276935, LC276936, LC276937 and LC276938 respectively, in NCBI, DDBJ and ENA by  Iraqi hereditary company. The result of translation by using BLASTx program showing that the amino acids of CRP for all patients decreased when compared with the standard samples of  less than 224 amino acids. The result of   ProtParam program that used for detection physio-chemical properties show that the mutations decreased the molecular weight of CRP for all patients when compared with the standard samples and also have an effect on the stability of CRP for patients with head and bone cancer make it unstable while the CRP of standard samples stable. The result of secondary structure prediction by using  PSIpred program showed that the mutation effected on the alpha helix, ß- turn and coil on CRP for all patients  when compared with the standard samples. The result of Phyre2 program showed that the mutation effected clearly  on the  tertiary structure for all patients when compared with the standard samples. The result of Swiss-model program for prediction quaternary structure of CRP was pentamer  (five subunit) for all patients and standard samples, except CRP for patient with poisoning thyroid gland consisted of one subunit.  

     While the result of STRING and Swiss-model programs for detecting the function of CRP showed the  same function of CRP for all patients and standard samples but, the mutations effected the activity defense of CRP for all patients by decreasing the number of calcium ions when compared with the standard samples. While the CRP for patient with poisoning thyroid gland  lost the function because it contained only one calcium ion. This results show that the mutations at gene level has large effected on translation process to protein and therefore have an effect on the physio-chemical properties, structure, activity and function of protein.