Sandbox Reserved 350: Difference between revisions
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*'''Apex 3'''—<font color='deeppink'>'''Gly75-Tyr84;''' Hydrophobic Loop (Leu79). </font> | *'''Apex 3'''—<font color='deeppink'>'''Gly75-Tyr84;''' Hydrophobic Loop (Leu79). </font> | ||
<Structure load='1czv' size='' frame='true' align='right' caption=' C2 Domain of Human Coagulation Factor V' scene='Sandbox_Reserved_350/Expriment3/2'>TextToBeDisplayed</scene>'/> | <Structure load='1czv' size='' frame='true' align='right' caption=' C2 Domain of Human Coagulation Factor V' scene='Sandbox_Reserved_350/Expriment3/2'>TextToBeDisplayed</scene>'/> | ||
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"/> | |||
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 '' | |||
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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 | ||
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The three loops are described by ''Macedo-Ribeiro et al.'' to protrude like spikes from the bottom of the barrel in monomeric FVa-C2.<ref name="Pubmed"/> It is also worth noting that spike (1) & spike (3) are separated by β-hairpin structures and spike (2) is described as a wider irregularly loop comparatively. These three loops extending from the C2 domain, are all linked to each other, and to '''three shorter loops''' by an intricate '''H-bonding network''' which extends to residues at the bottom of the β-barrel.<ref name="Pubmed"/> | The three loops are described by ''Macedo-Ribeiro et al.'' to protrude like spikes from the bottom of the barrel in monomeric FVa-C2.<ref name="Pubmed"/> It is also worth noting that spike (1) & spike (3) are separated by β-hairpin structures and spike (2) is described as a wider irregularly loop comparatively. These three loops extending from the C2 domain, are all linked to each other, and to '''three shorter loops''' by an intricate '''H-bonding network''' which extends to residues at the bottom of the β-barrel.<ref name="Pubmed"/> | ||
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The overall Barrel structure is closed at the top and bottom by | The overall Barrel structure is closed at the top and bottom by straight segments, giving it an overall spherical shape with a flattened upper surface. | ||
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