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Function of your protein

Converts P5C to proline. When complexed with NFLP, NFLP inhibits this function, interrupting the proline cycle in cancerous cells, and decreasing spheroid growth. ^[1]

Biological relevance and broader implications

PYCR-1 has been shown to have have many effects on the survival and proliferation of cancerous cells when the proline cycle is able to continue ^[2]. NFLP is a competitive inhibitor of PYCR-1. When NFLP is able to bind it changes the conformation of the protein, which in turn makes it unable to convert P5C to proline, and disrupts the proline cycle ^[3]. In this way, NFLP shows potential for further research into reducing the success of cancerous cells. Since NFLP is a competitive inhibitor, this means that some PYCR-1 protein will still bind P5C and partake in the proline cycle. NFLP then shows promise to reduce, but not eliminate the proliferation of cancer. Research should be done into any analogs of NFLP which could prove to be more successful inhibitors.

Important amino acids

When we look at the primary structure of the protein, there are specific amino acids important to the binding on NFLP. These amino acids are Histidine 223, Aspartic acid 229, Valine 231, Serine 233, and Alanine 237^[4].

Structural highlights

Other important features

The other unique feature that allows NFLP to bind more tightly than proline is that the alphaK helices rotate 1 angstrom, , and the helices glide past each other, which makes the molecule more capable of accommodating the formyl group of NFLP^[5].