User:Letícia Oliveira Rojas Cruz/Sandbox 1

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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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<scene name='10/1078774/Interacao_cation/1'>Polar cation-pi interactions</scene> occur between the amino acids '''{{Font color|turquoise|Arg652}}''' and '''{{Font color|slateblue|Tyr641}}''' of the opposite ACE2 molecule, and between '''{{Font color|turquoise|Arg710}}''' and '''{{Font color|slateblue|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.
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<scene name='10/1078774/Interacao_cation/1'>Polar cation-pi interactions</scene> occur between the amino acids '''{{Font color|slateblue|Arg652}}''' and '''{{Font color|turquoise|Tyr641}}''' of the opposite ACE2 molecule, and between '''{{Font color|slateblue|Arg710}}''' and '''{{Font color|turquoise|Tyr633}}'''. Additionally, <scene name='10/1078774/Lig_hidrogenio/1'>hydrogen bonds</scene> help stabilize the dimer interface: '''{{Font color|slateblue|Arg652}}''' forms a hydrogen bond with '''{{Font color|slateblue|Arg638}}''', which further interacts with '''{{Font color|slateblue|Gln653}}''', linked to '''{{Font color|turquoise|Asn636}}'''. Also, '''{{Font color|slateblue|Arg710}}''' forms a hydrogen bond with '''{{Font color|turquoise|Asn639}}''', and '''{{Font color|turquoise|Arg716}}''' connects with '''{{Font color|slateblue|Ser709}}''' and '''{{Font color|slateblue|Asp713}}'''.
'''''Domain PD Interation'''''
'''''Domain PD Interation'''''
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In addition to the CLD, the Peptidase Domain (PD) also contributes to ACE2 dimerization. The amino acids Cys133, Asn134, Asp136, Asn137, Gln139, Glu140, and Cys141 form a <scene name='10/1078774/Lig_hidrogenio/2'>loop</scene> region within the PD. The two cysteines (Cys133 and Cys141) establish a disulfide bond, which stabilizes the loop conformation, supported by additional intraloop polar interactions. Furthermore, Gln139 forms a polar interaction with Gln175 from the other ACE2 monomer.
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In addition to the CLD, the Peptidase Domain (PD) also contributes to ACE2 dimerization. The amino acids '''{{Font color|slateblue|Cys133}}''', '''{{Font color|slateblue|Asn134}}''', '''{{Font color|slateblue|Asp136}}''', '''{{Font color|slateblue|Asn137}}''', '''{{Font color|slateblue|Gln139}}''', '''{{Font color|slateblue|Glu140}}''', and '''{{Font color|slateblue|Cys141}}''' form a <scene name='10/1078774/Lig_hidrogenio/2'>loop</scene> region within the PD. The two cysteines ('''{{Font color|slateblue|Cys133}}''' and '''{{Font color|slateblue|Cys141}}''') establish a disulfide bond, which stabilizes the loop conformation, supported by additional intraloop polar interactions. Furthermore, '''{{Font color|slateblue|Gln139}}''' forms a polar interaction with '''{{Font color|turquoise|Gln175}}''' from the other ACE2 monomer.
=== SARS-CoV-2 Binding ===
=== SARS-CoV-2 Binding ===

Revision as of 22:35, 22 June 2025

Introduction

PDB 6m17

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Letícia Oliveira Rojas Cruz

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