Friday, April 18, 2014

P53 the super protein

Inevitably when taking any biochem class you going to encounter some cool proteins. There are proteins that look cool, proteins with cool sub-groups and proteins that have some cool chemistry involved. None of theses are even close to the awesome protein that is P53. Now I know what you are thinking, with a name so bland as P53 this protein has to suck. You couldn't be more wrong. P53 goes by many names "Tumor Suppressor Protein", "Guardian of the Genome", and "The Coolest Protein Ever". Are these names warranted? Absolutely.

STRUCTURE


In order to fully appreciate you need to start with the structure. P53 is flexible protein, so instead of all of those boring enzymes with fixed structures, P53 has a continually changing structure. That's right, it's too cool for X-ray crystallography. The best that scientists can do is determine a few rigid domains in the overall structure. First off, in the middle, is the tetramerization domain. If you thought one subunit could control this protein you were wrong. Second is the DNA binding domain. This is the part of the protein that binds directly to the most important molecule in your body, your DNA. Lastly is the transactivation domain, this domain helps the protein read your DNA. All together these three domains work in perfect unison creating the most amazing protein that your body has to offer.

FUNCTION

P53 is the most researched protein you will ever see. Why is this? It is because P53 stops cancer. That's right boys and girls, this protein stops cancer, how could you vote for anything else. If that wasn't enough lets go more in depth on exactly how it works. P53 is made just like any other protein. It is made by mRNA in the ribosome creating proteins. The difference between P53 and any other normal protein is that P53 turns right back around to the DNA whence it came, and starts telling it where it went wrong. P53 is literally too cool for DNA. So what happens when P53 sees some damaged DNA? It casually sends some signals, and stops the entire cell cycle. When P53 says stop the entire cell listens. But it just keeps getting cooler. It then tries to repair the DNA. Just for a little review you need to remember that DNA is what makes other proteins. P53 is the super protein that makes sure all the other proteins are in line, it's that big of a deal. But what happens if the DNA can't be repaired? Good question. P53 then sends signals for the cell to kill itself, and the cell does. P53 has the ability to kill the entire cell if it isn't happy. It's just that badass. 


REGULATION

Now before you go on thinking that P53 is regulated by some mere hormone or simple phosphorylation like other inferior proteins, you need to think. Would P53 really succumb to regulation that easily? Of course not, introducing MDM2. This isn't a hormone but an entire protein whose only job is to hold P53 back. When MDM2 is bound to P53 activity is lowered. In fact without MDM2 cells are unable to live because P53 is just too awesome to exist without regulation. So together MDM2 and P53 for a dynamic cancer fighting super duo that keeps your cells in check and out of trouble. Remember don't vote for any of the other boring proteins you see. Vote for the protein with the ability to kill an entire cell just because it's unhappy.  

Images:

-http://www.rcsb.org/pdb/101/motm.do?momID=31&evtc=Suggest&evta=Moleculeof%20the%20Month&evtl=TopBar

-http://upload.wikimedia.org/wikipedia/commons/9/9a/P53_pathways.jpg






3 comments:

  1. Hi Seth,

    My favorite part of your post was your enthusiasm. It was very infectious! You are definitely right, you've picked one of the world's coolest proteins.
    I also particularly liked your section on structure. It was very well written!
    I would only suggest that you include another figure or two and a little more detail. How does p53 know when DNA is damaged? To which part of p53 does MDM2 bind in order to inhibit it?

    Great job!
    Rian

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  2. Hey Seth!

    I love your energy through the entire blog. If anyone needs a laugh, they can just read your blog. I thought the first part of your blog with all the pictures you had created was absolutely hysterical! It all definitely grabs the reader's attention. I agree with Rian about adding some more figures, because who doesn't like figures, plus they also clarify one's understandings. Also, there are differences in the text size/font/color which can be distracting and looks like somethings were copied and pasted in. Overall, it was a lot of fun to read! Good job!

    Stephanie

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  3. Hi Seth,

    As other people said, I also could see the energy through your writing style. Specially when you said "that's right boy's and girl's." You did a good job, but if you talk little more about MDM2 will make your post better.

    Isaac Ahn

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