Sandbox Reserved 1627: Difference between revisions

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===Binding interactions===

[[Image:Binding site with AA labeled.png|thumb|right|270px|Figure 3: Subunit interactions between the insulin receptor CT-alpha helix (light blue) and insulin (magenta) in one of the binding sites. [http://www.rcsb.org/structure/6sof PDB 6SOF]]]

A tripartite interaction occurs between the alpha-CT chain and the FnIII-1 domain region during the conformational change. This interaction involves the following residues: <scene name='83/832953/Alpha_ct_and_fniii-1/7'>ASP496, ARG498, and ASP499 on the FnIII-1 domain</scene> and the <scene name='83/832953/Alpha_ct_and_fniii-1/5'>LYS703, GLU706, and ASP707 on the alpha-CT domain</scene>. This duo then interacts with the leucine rich region, L1, that exists on the opposing protomer of the dimer. The tripartite interaction between the alpha-CT chain and FnIII-1 domain on one dimer and the L1 region on the other dimer is important because it allows for a strong and stable interaction between two dimers of the insulin receptor that maintains the T-shape activation state for the rest of the downstream signaling to occur.

A tripartite interaction occurs between the alpha-CT chain and the FnIII-1 domain region during the conformational change. This interaction involves the following residues: <scene name='83/832953/Alpha_ct_and_fniii-1/7'>ASP496, ARG498, and ASP499 on the FnIII-1 domain</scene> and the <scene name='83/832953/Alpha_ct_and_fniii-1/9'>LYS703, GLU706, and ASP707 on the alpha-CT domain</scene>. This duo then interacts with the leucine rich region, L1, that exists on the opposing protomer of the dimer. The tripartite interaction between the alpha-CT chain and FnIII-1 domain on one dimer and the L1 region on the other dimer is important because it allows for a strong and stable interaction between two dimers of the insulin receptor that maintains the T-shape activation state for the rest of the downstream signaling to occur.

[[Image:4 sites highlighted.png|thumb|right|260px|Figure 4: The presence of all four potential binding sides on the active insulin receptor: sites 1 and 1' (green) and sites 2, and 2'(red). [http://www.rcsb.org/structure/6sof PDB 6SOF]]]

Sandbox Reserved 1627: Difference between revisions

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@@ Line 27: / Line 27: @@
 ===Binding interactions===
 [[Image:Binding site with AA labeled.png|thumb|right|270px|Figure 3: Subunit interactions between the insulin receptor CT-alpha helix (light blue) and insulin (magenta) in one of the binding sites. [http://www.rcsb.org/structure/6sof PDB 6SOF]]]
-A tripartite interaction occurs between the alpha-CT chain and the FnIII-1 domain region during the conformational change. This interaction involves the following residues: <scene name='83/832953/Alpha_ct_and_fniii-1/7'>ASP496, ARG498, and ASP499 on the FnIII-1 domain</scene> and the <scene name='83/832953/Alpha_ct_and_fniii-1/5'>LYS703, GLU706, and ASP707 on the alpha-CT domain</scene>. This duo then interacts with the leucine rich region, L1, that exists on the opposing protomer of the dimer. The tripartite interaction between the alpha-CT chain and FnIII-1 domain on one dimer and the L1 region on the other dimer is important because it allows for a strong and stable interaction between two dimers of the insulin receptor that maintains the T-shape activation state for the rest of the downstream signaling to occur.
+A tripartite interaction occurs between the alpha-CT chain and the FnIII-1 domain region during the conformational change. This interaction involves the following residues: <scene name='83/832953/Alpha_ct_and_fniii-1/7'>ASP496, ARG498, and ASP499 on the FnIII-1 domain</scene> and the <scene name='83/832953/Alpha_ct_and_fniii-1/9'>LYS703, GLU706, and ASP707 on the alpha-CT domain</scene>. This duo then interacts with the leucine rich region, L1, that exists on the opposing protomer of the dimer. The tripartite interaction between the alpha-CT chain and FnIII-1 domain on one dimer and the L1 region on the other dimer is important because it allows for a strong and stable interaction between two dimers of the insulin receptor that maintains the T-shape activation state for the rest of the downstream signaling to occur.
 [[Image:4 sites highlighted.png|thumb|right|260px|Figure 4: The presence of all four potential binding sides on the active insulin receptor: sites 1 and 1' (green) and sites 2, and 2'(red). [http://www.rcsb.org/structure/6sof PDB 6SOF]]]