BCL6 (Hebrew)

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==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='1R28' size='340' side='right' caption='Human Bcl-6 protein domain BTB (PDB code [[1r28]])' scene=''>
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<StructureSection load='1R28' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page '''BCL6 (Hebrew)'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Intorduction ==
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==מבנה ותפקוד האנזים==
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Green fluorescent protein ('''GFP'''), originally isolated from the jellyfish Aequorea victoria (PDB entry [[1ema]]), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.
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בעת פעולתו, האנזים RT מועד לטעויות. בניסוי<ref>Preston, B., Poiesz, B., & Loeb, L. (1988). Fidelity of HIV-1 Reverse Transcriptase. Science, 242(4882), 1168-1171. Retrieved from http://www.jstor.org/stable/1702640</ref> שנערך נמצא כי תדירות המוטציות במולקולת ה-DNA הנוצרת הוא 1 ל-4000-2000.
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משמעות הדבר היא שמתרחשת מוטציה אחת כל כשלושת אלפים נוקלאוטידים המתרכבים למולקולת ה-DNA הנוצרת. קצב המוטציות הגבוה גורם לכך שהחומר התורשתי של הנגיף משתנה כמעט עם כל הדבקה. עקב כך, מוטציות שמתרחשות במהלך פעולתו של אנזים RT גורמות לשינוי החומר הגנטי של הנגיף. דבר זה מאפשר לנגיף "להתחמק" מן המערכת החיסונית של המאכסן ולפתח עמידות נגד תרופות אנטי-ויראליות, ולכן פיתוח תרופות נגד הנגיף נתקל בקשיים רבים.
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== Exploring the Structure ==
 
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GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The chromophore, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.<ref>PMID:8703075</ref>
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== Function ==
 
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== Disease ==
 
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== Relevance ==
 
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== Structural highlights ==
 
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
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==Quiz==
 
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<quiz display=simple>
 
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{What do you think about Proteopedia <scene name="/12/3456/Sample/1">color</scene>?}
 
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- Nice
 
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- Okay
 
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+ So cool, I can't believe I didn't know about it before!
 
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- informative
 
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</quiz>
 
</StructureSection>
</StructureSection>
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== References ==
 
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<references/>
 

Current revision

Human Bcl-6 protein domain BTB (PDB code 1r28)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Nachum Nathan, Michal Harel

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