Sandbox42: Difference between revisions

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== '''Overall Structure''' ==

To date, the entire X-ray or NMR crystal structure of the <scene name='Sandbox42/Initial/1'>NMDA receptor</scene> has not been produced. However, there are many structural subunits of NMDA that have successfully been crystallized and analyzed which provide some structural information about the NMDA receptor. The architecture of NMDA receptors is modular and is composed of multiple domains with distinct functional roles. The large extracellular region of the receptor is partitioned into two domains: an <scene name='Sandbox42/Atd/1'>amino-terminal domain</scene> (ATD) and a <scene name='Sandbox42/Lbd/2'>ligand-binding domain</scene> (LBD) (7). Each domain consists of 8 <scene name='Sandbox42/Alpha/2'>alpha helices</scene> and antiparallel <scene name='Sandbox42/Beta/3'>beta sheets</scene>. The alpha helices are located on the outside while the beta sheets are found more toward the center.

To date, the entire X-ray or NMR crystal structure of the <scene name='Sandbox42/Initial/1'>NMDA receptor</scene> has not been produced. However, there are many structural subunits of NMDA that have successfully been crystallized and analyzed which provide some structural information about the NMDA receptor. The architecture of NMDA receptors is modular and is composed of multiple domains with distinct functional roles. The large extracellular region of the receptor is partitioned into two domains: an <scene name='Sandbox42/Atd/1'>amino-terminal domain</scene> (ATD) and a <scene name='Sandbox42/Lbd/2'>ligand-binding domain</scene> (LBD) (7). Each domain consists of 8 <scene name='Sandbox42/Alpha/2'>alpha helices</scene> and antiparallel <scene name='Sandbox42/Beta/3'>beta sheets</scene>. The alpha helices are located on the outside while the beta sheets are found more toward the center. The NMDA receptor has polar amino acid side-chains located extracellularly and at the ion-pore, but also many non-polar side chains at points where the protein passes through the phospholipid bilayer.

The ligand-binding domain of NMDA receptors are heterotetrameric ion channels composed of two copies of the glycine-binding NR1 subunit and two copies of the L-glutamate-binding NR2 subunit. The NR1 subunit is further divided up into splice units while the NR2 subunit has four sub-variants (NR2A-NR2D). The receptor as a whole has four general ligand binding sites (6).

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 == '''Overall Structure''' ==
-To date, the entire X-ray or NMR crystal structure of the <scene name='Sandbox42/Initial/1'>NMDA receptor</scene> has not been produced. However, there are many structural subunits of NMDA that have successfully been crystallized and analyzed which provide some structural information about the NMDA receptor. The architecture of NMDA receptors is modular and is composed of multiple domains with distinct functional roles. The large extracellular region of the receptor is partitioned into two domains: an <scene name='Sandbox42/Atd/1'>amino-terminal domain</scene> (ATD) and a <scene name='Sandbox42/Lbd/2'>ligand-binding domain</scene> (LBD) (7). Each domain consists of 8 <scene name='Sandbox42/Alpha/2'>alpha helices</scene> and antiparallel <scene name='Sandbox42/Beta/3'>beta sheets</scene>. The alpha helices are located on the outside while the beta sheets are found more toward the center.
+To date, the entire X-ray or NMR crystal structure of the <scene name='Sandbox42/Initial/1'>NMDA receptor</scene> has not been produced. However, there are many structural subunits of NMDA that have successfully been crystallized and analyzed which provide some structural information about the NMDA receptor. The architecture of NMDA receptors is modular and is composed of multiple domains with distinct functional roles. The large extracellular region of the receptor is partitioned into two domains: an <scene name='Sandbox42/Atd/1'>amino-terminal domain</scene> (ATD) and a <scene name='Sandbox42/Lbd/2'>ligand-binding domain</scene> (LBD) (7). Each domain consists of 8 <scene name='Sandbox42/Alpha/2'>alpha helices</scene> and antiparallel <scene name='Sandbox42/Beta/3'>beta sheets</scene>. The alpha helices are located on the outside while the beta sheets are found more toward the center. The NMDA receptor has polar amino acid side-chains located extracellularly and at the ion-pore, but also many non-polar side chains at points where the protein passes through the phospholipid bilayer.
 The ligand-binding domain of NMDA receptors are heterotetrameric ion channels composed of two copies of the glycine-binding NR1 subunit and two copies of the L-glutamate-binding NR2 subunit. The NR1 subunit is further divided up into splice units while the NR2 subunit has four sub-variants (NR2A-NR2D). The receptor as a whole has four general ligand binding sites (6).