Our project has been successful in meeting all of the objectives we set out to fulfill. We identified our gene with 100% query match to be B-Raf proto-oncogene, serine/threonine kinase in Homo sapiens. Using the databases and techniques discussed in tools and methods, we were also able to find the structure of the gene and its differing isoforms. Using this information, we constructed gene and isoform diagrams that are to scale. We were also able to discover the many different tissues that BRAF is found in, which include cancerous tissues and fast dividing tissues such as the testis, stomach, and many others. The protein structure, function, and biochemical pathways were also thoroughly analyzed using information from a plethora of databases and websites. By discovering this information about the protein, we could better understand why malfunctions of it will lead to the various disease described in the mutations and disease association section.
Gene
Our gene is a human B-Raf proto-oncogene, serine/threonine kinase that has five different known isoforms. This gene is found in chromosome 7 and has 190,753 base pairs which code for 766 amino acids. The gene was found to be expressed in thirty different tissues, which indicats just how important it is to the healthy function of the body. Only one of the isoforms found was able to code for a protein, while the others were truncated by nonsense mediated decay. All of the isoforms differ significantly in their number of exons, which shows the limits in alternative expression for this gene as it needs to be transcribed and translated as accurately as possible to function correctly within the tissues.
Protein Structure and Function
B-raf protein is a clear example of the common biological theme of structure meeting function. Understanding Braf as a Raf protein and the relationships of its domains to larger categories of domains shows the relationship of Braf to other protein kinases. The importance of its ATP binding domain and its location relative to the larger conserved kinase domain of B-raf allowed for a greater understanding of B-raf phosphorylating mechanisms. B-raf's tendency to sometimes homodimerize or heterodimerize presents more challenges to understanding its mechanism, and requires greater research.
Mutations and Disease Association
As a protein involved in the MAPK signaling pathway, which helps to regulate processes of cell proliferation and death, mutations in B-raf prove to be very dangerous. The most common B-raf mutation, V600E, is a marker for numerous types of cancers, and other mutations also contribute to cancers as well as other diseases. The issue of B-raf inhibition not preventing its phosphorylating activity has led to curing and managing these diseases more difficult, since inhibition of this key phosphorylator would have had an effect had it not been for its dimeric activity that increases its phosphorylation efficiency.