Sandbox Reserved 1170: Difference between revisions

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=== ECL2 ===

Although it may be different in many ways, hGPR40 is similar to most G protein coupled receptors because it contains a highly conserved hairpin loop. This extracellular loop (<scene name='72/721541/Ecl2/2'>ECL2</scene>), is accompanied by a [https://en.wikibooks.org/wiki/Structural_Biochemistry/Chemical_Bonding/_Disulfide_bonds disulfide bond] and serves an important role in the protein. In hGPR40, ECL2 has two sections: a beta sheet and an auxiliary loop. The [https://en.wikipedia.org/wiki/Beta_sheet beta sheet] (shown in cyan) spans helices 4 and 5. The ECL2 of hGPR40 differs from that of other proteins because it contains an auxiliary loop (magenta) of 13 extra residues. The entire extracellular loop has low mobility and flexibility which allows it to act as a cap for the binding pocket. The only exception to the low flexibility is the tip of the auxiliary loop, which corresponds to residues Asp 152-Asn 155. This area of greater mobility allows for substrates to enter the binding site.<ref name="Srivastava"/>

Although it may be different in many ways, hGPR40 is similar to most G protein coupled receptors because it contains a highly conserved hairpin loop. This extracellular loop (<scene name='72/721541/Ecl2/3'>ECL2</scene>), is accompanied by a [https://en.wikibooks.org/wiki/Structural_Biochemistry/Chemical_Bonding/_Disulfide_bonds disulfide bond] and serves an important role in the protein. In hGPR40, ECL2 has two sections: a beta sheet and an auxiliary loop. The [https://en.wikipedia.org/wiki/Beta_sheet beta sheet] (shown in cyan) spans helices 4 and 5. The ECL2 of hGPR40 differs from that of other proteins because it contains an auxiliary loop (magenta) of 13 extra residues. The entire extracellular loop has low mobility and flexibility which allows it to act as a cap for the binding pocket. The only exception to the low flexibility is the tip of the auxiliary loop, which corresponds to residues Asp 152-Asn 155. This area of greater mobility allows for substrates to enter the binding site.<ref name="Srivastava"/>

== Function ==

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 === ECL2 ===
-Although it may be different in many ways, hGPR40 is similar to most G protein coupled receptors because it contains a highly conserved hairpin loop. This extracellular loop (<scene name='72/721541/Ecl2/2'>ECL2</scene>), is accompanied by a [https://en.wikibooks.org/wiki/Structural_Biochemistry/Chemical_Bonding/_Disulfide_bonds disulfide bond] and serves an important role in the protein. In hGPR40, ECL2 has two sections: a beta sheet and an auxiliary loop. The [https://en.wikipedia.org/wiki/Beta_sheet beta sheet] (shown in cyan) spans helices 4 and 5. The ECL2 of hGPR40 differs from that of other proteins because it contains an auxiliary loop (magenta) of 13 extra residues. The entire extracellular loop has low mobility and flexibility which allows it to act as a cap for the binding pocket. The only exception to the low flexibility is the tip of the auxiliary loop, which corresponds to residues Asp 152-Asn 155. This area of greater mobility allows for substrates to enter the binding site.<ref name="Srivastava"/>
+Although it may be different in many ways, hGPR40 is similar to most G protein coupled receptors because it contains a highly conserved hairpin loop. This extracellular loop (<scene name='72/721541/Ecl2/3'>ECL2</scene>), is accompanied by a [https://en.wikibooks.org/wiki/Structural_Biochemistry/Chemical_Bonding/_Disulfide_bonds disulfide bond] and serves an important role in the protein. In hGPR40, ECL2 has two sections: a beta sheet and an auxiliary loop. The [https://en.wikipedia.org/wiki/Beta_sheet beta sheet] (shown in cyan) spans helices 4 and 5. The ECL2 of hGPR40 differs from that of other proteins because it contains an auxiliary loop (magenta) of 13 extra residues. The entire extracellular loop has low mobility and flexibility which allows it to act as a cap for the binding pocket. The only exception to the low flexibility is the tip of the auxiliary loop, which corresponds to residues Asp 152-Asn 155. This area of greater mobility allows for substrates to enter the binding site.<ref name="Srivastava"/>
 == Function ==