Abnormal serine phosphorylation of the insulin receptor or insulin receptor substrate proteins is a prime candidate.
Incorporating CpTI into assays using fluorogenic substrates we were able to show that the serine PI inhibited the activity of the refolded proteinases.
Serine Protease In the diagram above a small peptide is shown being cleaved, while the usual substrate would be a larger polypeptide.
The figure shows a crystal of the amino acid serine in a high pressure cell.
The function of t-PA is to cleave a particular peptide bond in plasminogen, forming plasmin (which is itself a serine protease ).
The modification, known as phosphorylation, occurs at a single amino-acid residue in H2AX known as a serine.
The overall mechanism of catalysis reaction by thiol proteinases is the same as in serine proteinases.
The predicted catalytic serine, histidine and aspartic acid residues are shown in ball-and-stick representation.
The serine protease factor B is central in the alternative pathway of activation.
The two proteases trypsin and chymotrypsin are grouped into the serine protease family.
These pure lecithin granules are a natural source of phosphatidyl serine (PS) an important nutrient for brain health.
This is the case in the trypsin family of serine proteases, examined in more detail later in this section.
Virtual northern data was collected for all three of the H. glycines serine proteinases in addition to that of G. pallida.
We are studying the structural biology of members of the serpin family of serine proteinase inhibitors using X-ray crystallography.
You could have a hydrogen bond set up between two serine residues in different parts of a folded chain.