Sandbox Reserved 350: Difference between revisions
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The apexes of these <font color='orangered'> '''three loops''' </font> within the C2 domain, are able to create a deep groove lined by '''hydrophobic''' <font color='brown'> '''(Trp31, Met83)''' </font> and '''polar residues''' <font color='royalblue'> '''(Gln48, Ser78)'''</font>, as seen and consisting the <scene name='Sandbox_Reserved_350/Expriment3/3'> | The apexes of these <font color='orangered'> '''three loops''' </font> within the C2 domain, are able to create a deep groove lined by '''hydrophobic''' <font color='brown'> '''(Trp31, Met83)''' </font> and '''polar residues''' <font color='royalblue'> '''(Gln48, Ser78)'''</font>, as seen and consisting the <scene name='Sandbox_Reserved_350/Expriment3/3'> Open Form </scene> of FVa-C2. This groove is seen as the primary membrane-binding site of the C2-Domain. <ref name="Pubmed"/> | ||
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A second dimeric crystal form of FVa-C2, packed through the free edges of S6 strands, presenting a different Leu104-Val109 | A second dimeric crystal form of FVa-C2, packed through the free edges of S6 strands, presenting a different Leu104-Val109 | ||
