User:Letícia Oliveira Rojas Cruz/Sandbox 1

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=== ACE2-B0AT1 Complex ===
=== ACE2-B0AT1 Complex ===
'''''Association with B0AT1'''''
'''''Association with B0AT1'''''
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The ACE2 protein can associate with the neutral amino acid transporter <scene name='10/1078774/B0at1_zoom2/1'>B0AT1</scene>, also known as SLC6A19. In this context, ACE2 first forms a <scene name='10/1083732/Dimer_ace2_final/1'>homodimer</scene>, where two ACE2 molecules interact side by side. Each ACE2 monomer then binds to one B0AT1 molecule. This results in a complex composed of '''{{Font color|darkviolet|two ACE2}}''' and '''{{Font color|salmon|two B0AT1}}''' molecules, which is commonly described as a <scene name='10/1083732/Ace2_and_b0at1/1'>dimer of heterodimers</scene>. This association is essential for the transport of neutral amino acids in intestinal cells and the anchoring of ACE2 in the cell membrane, keeping the catalytic site facing the extracellular environment. Although ACE2 dimerization occurs independently of B0AT1, the transporter plays a stabilizing role by interacting with the Collectrin-like Domain.
The ACE2 protein can associate with the neutral amino acid transporter <scene name='10/1078774/B0at1_zoom2/1'>B0AT1</scene>, also known as SLC6A19. In this context, ACE2 first forms a <scene name='10/1083732/Dimer_ace2_final/1'>homodimer</scene>, where two ACE2 molecules interact side by side. Each ACE2 monomer then binds to one B0AT1 molecule. This results in a complex composed of '''{{Font color|darkviolet|two ACE2}}''' and '''{{Font color|salmon|two B0AT1}}''' molecules, which is commonly described as a <scene name='10/1083732/Ace2_and_b0at1/1'>dimer of heterodimers</scene>. This association is essential for the transport of neutral amino acids in intestinal cells and the anchoring of ACE2 in the cell membrane, keeping the catalytic site facing the extracellular environment. Although ACE2 dimerization occurs independently of B0AT1, the transporter plays a stabilizing role by interacting with the Collectrin-like Domain.
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In this region, there is an extensive network of polar interactions that stabilizes the ACE2 dimer. The most actively involved amino acid residues are between 636 and 658 and between 708 and 717, corresponding to the second and fourth helices of the CLD domain, respectively.
In this region, there is an extensive network of polar interactions that stabilizes the ACE2 dimer. The most actively involved amino acid residues are between 636 and 658 and between 708 and 717, corresponding to the second and fourth helices of the CLD domain, respectively.
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Polar cation-π interactions occur between the amino acids Arg652 and Tyr641 of the opposite ACE2 molecule, and between Arg710 and Tyr633. Additionally, hydrogen bonds help stabilize the dimer interface: Arg652 forms a hydrogen bond with Asn638, which further interacts with Gln653, linked to Asn636. Also, Arg710 forms a hydrogen bond with Glu639, and Arg716 connects with Ser709 and Asp713.
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<scene name='10/1078774/Interacao_cation/1'>Polar cation-pi interactions</scene> occur between the amino acids Arg652 and Tyr641 of the opposite ACE2 molecule, and between Arg710 and Tyr633. Additionally, <scene name='10/1078774/Lig_hidrogenio/1'>hydrogen bonds</scene> help stabilize the dimer interface: Arg652 forms a hydrogen bond with Asn638, which further interacts with Gln653, linked to Asn636. Also, Arg710 forms a hydrogen bond with Glu639, and Arg716 connects with Ser709 and Asp713.
'''''Domain PD Interation'''''
'''''Domain PD Interation'''''

Revision as of 21:49, 22 June 2025

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PDB 6m17

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Letícia Oliveira Rojas Cruz

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