Sandbox Reserved 1649: Difference between revisions

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NR1 and NR2A are assembled in a dimer, arranged in a back-to-back fashion, thanks to interactions between three different domains on each subunit: sites I, II and III.

- Site II: The link between NR2A and NR1 is made by at least three amino acids: E530 (<scene name='86/868182/E68/1'>E68 in LBD</scene>) makes a salt bridge with R755 of NR1, F524 (<scene name='86/868182/F62/1'>F62 in LBD</scene>) binds K531 of NR1 by a hydrogen bond on the backbone carbonyl oxygen, and P257.

- Site II: The link between NR2A and NR1 is made by at least three amino acids: E530 (<scene name='86/868182/E68/1'>E68 in LBD</scene>) makes a salt bridge with R755 of NR1, F524 (<scene name='86/868182/F62/1'> F62 in LBD</scene>) binds K531 of NR1 by a hydrogen bond on the backbone carbonyl oxygen, and P257.

- Sites I and III: the binding is established by hydrophobic residues (I514 (<scene name='86/868182/I52/1'>I52 in LBD</scene>), V526 (<scene name='86/868182/V64/1'>V64 in LBD</scene>), L777, L780 present on helices D and J), or by polar contacts

- Sites I and III: the binding is established by hydrophobic residues (I514 (<scene name='86/868182/I52/1'> I52 in LBD</scene>), V526 (<scene name='86/868182/V64/1'>V64 in LBD</scene>), L777, L780 present on helices D and J), or by polar contacts

Depending on the kind of NR2 (A-D) linked to NR1, the affinity of NR1 for glycine can be affected. Moreover, for a particular combination of NR1 and NR2 subunits, a negative cooperativity has been observed between glycine and glutamate binding. This leads to consider a possible allosteric coupling between NR1 and NR2. Thus, the importance of the structure of NR2A to make contacts with NR1 is obvious. But mechanistic explanation about the role that subunit-subunit contacts might have in NMDA receptor activity has not been found yet.

Sandbox Reserved 1649: Difference between revisions

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 NR1 and NR2A are assembled in a dimer, arranged in a back-to-back fashion, thanks to interactions between three different domains on each subunit: sites I, II and III.
--	Site II: The link between NR2A and NR1 is made by at least three amino acids: E530 (<scene name='86/868182/E68/1'>E68 in LBD</scene>) makes a salt bridge with R755 of NR1, F524 (<scene name='86/868182/F62/1'>F62 in LBD</scene>) binds K531 of NR1 by a hydrogen bond on the backbone carbonyl oxygen, and P257.
+-	Site II: The link between NR2A and NR1 is made by at least three amino acids: E530 (<scene name='86/868182/E68/1'>E68 in LBD</scene>) makes a salt bridge with R755 of NR1, F524 (<scene name='86/868182/F62/1'> F62 in LBD</scene>) binds K531 of NR1 by a hydrogen bond on the backbone carbonyl oxygen, and P257.
--	Sites I and III: the binding is established by hydrophobic residues (I514 (<scene name='86/868182/I52/1'>I52 in LBD</scene>), V526 (<scene name='86/868182/V64/1'>V64 in LBD</scene>), L777, L780 present on helices D and J), or by polar contacts
+-	Sites I and III: the binding is established by hydrophobic residues (I514 (<scene name='86/868182/I52/1'> I52 in LBD</scene>), V526 (<scene name='86/868182/V64/1'>V64 in LBD</scene>), L777, L780 present on helices D and J), or by polar contacts
 Depending on the kind of NR2 (A-D) linked to NR1, the affinity of NR1 for glycine can be affected. Moreover, for a particular combination of NR1 and NR2 subunits, a negative cooperativity has been observed between glycine and glutamate binding. This leads to consider a possible allosteric coupling between NR1 and NR2. Thus, the importance of the structure of NR2A to make contacts with NR1 is obvious. But mechanistic explanation about the role that subunit-subunit contacts might have in NMDA receptor activity has not been found yet.