Sandbox 37

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<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Matt's Beautiful Protein' />
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='''Interferon-β'''=
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The <scene name='Sandbox_37/Matt_adenylate_kinase_37/1'>Adenylate Kinase</scene> protein is shown here with alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange).
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===Introduction===
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The <scene name='Sandbox_37/Matt_helix_beta_colored/1'>Secondary Structure</scene> of the protein is shown here with alpha helices (green) and beta sheets (blue) highlighted appropriately.
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Interferon-β is a protein growth factor that stimulates an antiviral defense. Its encoding gene is one of only two known vertebrate structural genes that lacks introns.<ref name="Biochem Text">Voet, D., Voet, J.G., and C. Pratt. ''Fundamentals of Biochemistry'' 3rd Edition. Hoboken, NJ: John Wiley and Sons, 2008. Print.</ref>
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The <scene name='Sandbox_37/Matt_hydrogen_bonds_good/1'>Hydrogen Bonds</scene> of chain A of the protein are highlighted in orange here.
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===History===
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==Structure==
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<Structure load='1IFA' size='400' frame='true' align='center' caption='Interferon-β' scene='Sandbox_37/Interferon_beta/4' />
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The <scene name='Sandbox_37/Matt_hydrophobic_good/1'>Hydrophobic Interactions</scene> are shown here in red.
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Interferon-β is a relatively simple biological response modifier, with several <scene name='Sandbox_37/Interferon_beta/2'>identifiable regions</scene>. It consists of five <scene name='Sandbox_37/Ifnb_helices_in_color/1'>alpha helices</scene>, as well as multiple interconnecting <scene name='Sandbox_37/Ifnb_loopregions_in_color/1'>loop regions</scene>. Helices A, B and D run <scene name='Sandbox_37/Ifnb_parallel_abd/1'>parallel to one another</scene>, and helices C and E run <scene name='Sandbox_37/Interferon_beta/3'>anti-parallel</scene> to the other three helices. Helix A consists of residues 6-23; Helix B consists of residues 49-65; Helix C consists of residues 77-91; Helix D consists of residues 112-131; and Helix E consists of residues 135-155.
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The <scene name='Sandbox_37/Matt_hydrophilic_good/1'>Hydrophilic Interactions</scene> are shown here in black.
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<ref name="Structure">PMID:20616576</ref>
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<ref name="UniProt">http://www.uniprot.org/uniprot/P00784</ref>
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The <scene name='Sandbox_37/Matt_solvent/1'>Solvent</scene> , which is water, is shown here in red. Water's primary location is on the outer parts of the protein, or the hydrophilic regions.
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===Solvent Interactions===
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The side chains that interact with the <scene name='Sandbox_37/Matt_ligand/1'>ligand</scene> are shown here in crimson. The interactions occur with the hydrophobic side chains. The rest of the protein is faded blue.
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===Mechanism===
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The <scene name='Sandbox_37/Matt_catalytic_residues/1'>catalytic residues</scene> of this protein are shown here in lime green.
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==Inhibition==
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===Inhibitors of Interferon-β===
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===Interferon-β as an Inhibitor===
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==Function==
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===Biochemical===
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===Immunological===
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==References==
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<references />
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Current revision

Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.

Adenylate Kinase

Drag the structure with the mouse to rotate

The protein is shown here with alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange).

The of the protein is shown here with alpha helices (green) and beta sheets (blue) highlighted appropriately.

The of chain A of the protein are highlighted in orange here.

The are shown here in red.

The are shown here in black.

The , which is water, is shown here in red. Water's primary location is on the outer parts of the protein, or the hydrophilic regions.

The side chains that interact with the are shown here in crimson. The interactions occur with the hydrophobic side chains. The rest of the protein is faded blue.

The of this protein are shown here in lime green.

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