Beta-2 adrenergic receptor: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Tala Curry, Michal Harel, Jaime Prilusky, Joel L. Sussman, Alexander Berchansky

@@ Line 26: / Line 26: @@
 ===Secondary===
-The secondary structure of CB1 consists 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.
+The secondary structure of CB1 consists 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>