Sandbox Reserved 1700: Difference between revisions

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[[Image:Agonists - Copy.png|400px|left|thumb|'''Figure 7.''' Agonists of MRGPRX2 due to their structural similarities to known ligands. Positive regions shown in blue and hydrophobic regions in green. Cortistatin-14, PAMP-12, and Zinc-3573 are all known to bind to MRGPRX2 with high affinity, and inhibit mast cell degranulation<ref name="Yang">PMID: 34789875</ref><ref name="Cao">PMID: 34789874</ref>]]
[[Image:Agonists - Copy.png|400px|right|thumb|'''Figure 7.''' Agonists of MRGPRX2 due to their structural similarities to known ligands. Positive regions shown in blue and hydrophobic regions in green. Cortistatin-14, PAMP-12, and Zinc-3573 are all known to bind to MRGPRX2 with high affinity, and inhibit mast cell degranulation<ref name="Yang">PMID: 34789875</ref><ref name="Cao">PMID: 34789874</ref>]]
Other endogenous compounds that share similar characteristics of these ligands are [https://pubchem.ncbi.nlm.nih.gov/compound/95882507 Zinc-3573], [https://pubchem.ncbi.nlm.nih.gov/compound/PAMP-12-_human_-porcine#section=Structures PAMP-12], and [https://pubchem.ncbi.nlm.nih.gov/compound/44208884 Cortistatin-14]. These molecules are known agonists of MRGPRX2 and bind similarly to sub-pockets 1 and 2.  
Other endogenous compounds that share similar characteristics of these ligands are [https://pubchem.ncbi.nlm.nih.gov/compound/95882507 Zinc-3573], [https://pubchem.ncbi.nlm.nih.gov/compound/PAMP-12-_human_-porcine#section=Structures PAMP-12], and [https://pubchem.ncbi.nlm.nih.gov/compound/44208884 Cortistatin-14]. These molecules are known agonists of MRGPRX2 and bind similarly to sub-pockets 1 and 2.  
An endogenous peptide, <scene name='90/904306/C-14_in_site/4'>Cortistatin-14</scene> models these interactions, binding to sub-pocket 1 through LYS-3 and sub-pocket 2 through hydrophobic interactions.
An endogenous peptide, <scene name='90/904306/C-14_in_site/4'>Cortistatin-14</scene> models these interactions, binding to sub-pocket 1 through LYS-3 and sub-pocket 2 through hydrophobic interactions.