Sandbox 420: Difference between revisions
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==Structure== | ==Structure== | ||
Primary: The cannabinoid receptor (CB1) has a total of 472 amino acids. Of the 472 amino acids, 52.75% are nonpolar, 26.91% are uncharged polar, and 20.34% are polar (12.08% basic and 8.26% acidic). | '''Primary:''' The cannabinoid receptor (CB1) has a total of 472 amino acids. Of the 472 amino acids, 52.75% are nonpolar, 26.91% are uncharged polar, and 20.34% are polar (12.08% basic and 8.26% acidic). | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'> | ||
</td></tr><tr id='Nonpolar Amino Acids Residues'><td class="sblockLbl"><b>[[Nonpolar Amino Acids Residues:]]</b></td><td class="sblockDat"><scene name='71/716602/Alanine_residues/2'>Ala </scene>,<scene name='71/716602/Phe/1'>Phe</scene>,<scene name='71/716602/Gly/1'>Gly</scene>,<scene name='71/716602/Ile/1'>Ile</scene>,<scene name='71/716602/Leu/1'>Leu</scene>,<scene name='71/716602/Met/1'>Met</scene>,<scene name='71/716602/Pro/1'>Pro</scene>,<scene name='71/716602/Val/1'>Val</scene>,<scene name='71/716602/Trp/1'>Trp</scene></td></tr> | </td></tr><tr id='Nonpolar Amino Acids Residues'><td class="sblockLbl"><b>[[Nonpolar Amino Acids Residues:]]</b></td><td class="sblockDat"><scene name='71/716602/Alanine_residues/2'>Ala </scene>,<scene name='71/716602/Phe/1'>Phe</scene>,<scene name='71/716602/Gly/1'>Gly</scene>,<scene name='71/716602/Ile/1'>Ile</scene>,<scene name='71/716602/Leu/1'>Leu</scene>,<scene name='71/716602/Met/1'>Met</scene>,<scene name='71/716602/Pro/1'>Pro</scene>,<scene name='71/716602/Val/1'>Val</scene>,<scene name='71/716602/Trp/1'>Trp</scene></td></tr> | ||
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[[Image:Cannabinoid_Receptor_1_Amino_Acid_Residues1.png]] | [[Image:Cannabinoid_Receptor_1_Amino_Acid_Residues1.png]] | ||
Secondary: The secondary structure of CB1 is made up of of ten <scene name='71/716602/Alpha_helices/1'>α-helices</scene> and one <scene name='71/716602/Beta_sheet/1'>β-sheet</scene>. Of the ten α-helices, eight are roughly identical in size and align parallel to one another to form a typical transmembrane-type domain. The remaining two α-helices are shorter in length, run perpendicular to the other eight, and are located at one end of the receptor. On the opposite end of the receptor, an antiparallel β-sheet is located in the middle of the transmembrane domain formed by the eight parallel helices. While the structure overall has a low composition of polar amino acids, a large portion are located within this β-sheet, hinting at the role it may play in the function of the receptor. | '''Secondary:''' The secondary structure of CB1 is made up of of ten <scene name='71/716602/Alpha_helices/1'>α-helices</scene> and one <scene name='71/716602/Beta_sheet/1'>β-sheet</scene>. Of the ten α-helices, eight are roughly identical in size and align parallel to one another to form a typical transmembrane-type domain. The remaining two α-helices are shorter in length, run perpendicular to the other eight, and are located at one end of the receptor. On the opposite end of the receptor, an antiparallel β-sheet is located in the middle of the transmembrane domain formed by the eight parallel helices. While the structure overall has a low composition of polar amino acids, a large portion are located within this β-sheet, hinting at the role it may play in the function of the receptor. | ||
<scene name='71/716602/Normal/1'>Initial Scene (Reset)</scene> | <scene name='71/716602/Normal/1'>Initial Scene (Reset)</scene> | ||
'''Tertiary:''' A homology model for the tertiary structure of CB1 is shown in the upper righthand of the page with the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> | |||
<ref>PMID:21638687</ref>. | |||
==Mechanism== | ==Mechanism== | ||
