Sandbox Reserved 1067: Difference between revisions

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== Structure ==

Yiip's complete protein structure is identified as a dimer. Each monomer structure is classified into two different domains, the Trans-Membrane Domain (TMD) and C-~~terminus~~ Domain (CTD). The TMD consists of six helices, forming binding site A, four of which are oriented in a parallel manner, with respect to each other, while the remaining two are aligned anti parallel to this four helix cluster. A "<scene name='69/694234/Bridge/1'>salt bridge</scene>" or "charge interlock" consisting of four amino acid residues, two Lysines (Lys 77) and two Aspartates (Asp 207), forms a junction that both monomers of Yiip converge at, forming a pivot point for conformation changes. A large portion of the protein containing binding site C, approximately 30 Å in length<sup>[1]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.

Yiip's complete protein structure is identified as a dimer. Each monomer structure is classified into two different domains, the Trans-Membrane Domain (TMD) and C-Terminus Domain (CTD). The TMD consists of six helices, forming binding site A, four of which are oriented in a parallel manner, with respect to each other, while the remaining two are aligned anti parallel to this four helix cluster. A "<scene name='69/694234/Bridge/1'>salt bridge</scene>" or "charge interlock" consisting of four amino acid residues, two Lysines (Lys 77) and two Aspartates (Asp 207), forms a junction that both monomers of Yiip converge at, forming a pivot point for conformation changes. A large portion of the protein containing binding site C, approximately 30 Å in length<sup>[1]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.

== Salt Bridge ==

Sandbox Reserved 1067: Difference between revisions

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 == Structure ==
-Yiip's complete protein structure is identified as a dimer. Each monomer structure is classified into two different domains, the Trans-Membrane Domain (TMD) and C-terminus Domain (CTD). The TMD consists of six helices, forming binding site A, four of which are oriented in a parallel manner, with respect to each other, while the remaining two are aligned anti parallel to this four helix cluster. A "<scene name='69/694234/Bridge/1'>salt bridge</scene>" or "charge interlock" consisting of four amino acid residues, two Lysines (Lys 77) and two Aspartates (Asp 207), forms a junction that both monomers of Yiip converge at, forming a pivot point for conformation changes. A large portion of the protein containing binding site C, approximately 30 Å in length<sup>[1]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.
+Yiip's complete protein structure is identified as a dimer. Each monomer structure is classified into two different domains, the Trans-Membrane Domain (TMD) and C-Terminus Domain (CTD). The TMD consists of six helices, forming binding site A, four of which are oriented in a parallel manner, with respect to each other, while the remaining two are aligned anti parallel to this four helix cluster. A "<scene name='69/694234/Bridge/1'>salt bridge</scene>" or "charge interlock" consisting of four amino acid residues, two Lysines (Lys 77) and two Aspartates (Asp 207), forms a junction that both monomers of Yiip converge at, forming a pivot point for conformation changes. A large portion of the protein containing binding site C, approximately 30 Å in length<sup>[1]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.
 == Salt Bridge ==