Sandbox 128: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Student, Allison Granberry

@@ Line 32: / Line 32: @@
 ==='''B-Lactams that Inhibit PBP2a'''===
-MRSA becomes resistant to almost all B-Lactams by acquiring an alternative TP, PBP2a, that is neither bound nor inhibited by B-Lactams. Recently, two cephlosporins- <scene name='37/372728/Ceftobiprole/3'>ceftobiprole</scene> and ceftaroline- that have anti-MRSA activity have been developed. Ceftobiprole is able to inhibit PBP2a because additional chemical groups at the <scene name='37/372728/R2_group/8'>R2</scene> position of ceftobiprole are able to interact with additional amino acid residues in PBP2a; specifically
+MRSA becomes resistant to almost all B-Lactams by acquiring an alternative TP, PBP2a, that is neither bound nor inhibited by B-Lactams. Recently, two cephlosporins- <scene name='36/365380/Ceftobiprole/28'>ceftobiprole</scene> and ceftaroline- that have anti-MRSA activity have been developed. Ceftobiprole is able to inhibit PBP2a because additional chemical groups at the <scene name='36/365380/Ceftobiprole/29'>R2</scene> position of ceftobiprole are able to interact with additional amino acid residues in PBP2a; specifically <scene name='37/372728/Tyr446_met641_interaction/4'>Tyr446 and Met641, and increase the association of ceftobiprole with PBP2a</scene>. As such, ceftobiprole is (shown as colors of the atom types [[CPK]]) is able to more efficiently react with Ser403 and therefore inhibit the activity of PBP2a.
-<scene name='37/372728/Tyr446_met641_interaction/4'>Tyr446 and Met641, and increase the association of ceftobiprole with PBP2a</scene>.
-As such, ceftobiprole is (shown as colors of the atom types [[CPK]]) is able to more efficiently react with Ser403 and therefore inhibit the activity of PBP2a.
@@ Line 45: / Line 43: @@
 Allosteric site serves as a binding site for the substrate <scene name='36/365380/3zfz_1/25'>peptidoglycan</scene>. When the substrate binds to the <scene name='36/365380/3zfz_1/21'>allosteric site</scene> (Tyr105, Asn146, Asp295, Tyr297), a conformational change occurs at the active site, opening it and allowing catalytic action to occur.
-The medicine, <scene name='36/365380/3zfz_1/24'>ceftaroline</scene>, mimics the substrate at the allosteric site opening the active site, allowing <scene name='36/365380/3zfz_1/22'>ceftaroline</scene> to <scene name='36/365380/3zfz_1/23'>enter and bind noncovalently</scene>.
+The medicine, <scene name='37/372728/Ceftaroline/2'>ceftaroline</scene>, mimics the substrate at the <scene name='37/372728/3zfz_allosteric_site/2'>allosteric site</scene> opening the active site, allowing <scene name='36/365380/3zfz_1/22'>ceftaroline</scene> to <scene name='36/365380/3zfz_1/23'>enter and bind noncovalently</scene>.