User:David Canner/Sandbox 2

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[[Image: Nexium.jpg|300px|right|thumb| AstraZeneca’s Nexium]]
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<big>The following is a list of major phamerceutical compound targets, organized by disease. </big>
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==Alzheimer’s Disease==
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[[Acetylcholinesterase]] <br />
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[[Amyloid Beta]]<br />
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[[Gamma-Secratase]]<br />
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[[Glutamate receptor (GluA2)]]<br />
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==Anemia==
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[[Erythropoietin]]<br />
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'''Hemoglobin''' is an oxygen-transport protein. Hemoglobin is an [[allosteric protein]]. It is a tetramer composed of two types of subunits designated α and β, with stoichiometry <scene name='Hemoglobin/Alpha2beta2/7'>α2β2</scene>. The
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==Asthma and other Pulmonary Disease States==
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<scene name='Hemoglobin/Foursubunits/5'>four subunits</scene> of hemoglobin sit roughly at the corners of a tetrahedron, facing each other across a <scene name='Hemoglobin/Cavity/9'>cavity</scene> at the center of the molecule. Each of the subunits <scene name='Hemoglobin/Bbsubunitswithheme/5'>contains a heme</scene> prosthetic group. The <scene name='Hemoglobin/4heme/3'>heme molecules</scene> give hemoglobin its red color.
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[[Beta-2-Andrenergic Receptor]]<br />
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[[Leukotriene Receptor]]<br />
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Each individual <scene name='Hemoglobin/Deoxyheme/8'>heme</scene> molecule contains one
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==Autoimmune Diseases==
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<scene name='Hemoglobin/Deoxyheme_fe/9'>Fe2+</scene> atom. In the lungs, where oxygen is abundant, an <scene name='Hemoglobin/Oxyheme_fe/7'>oxygen molecule</scene> binds to the ferrous iron atom of the heme molecule and is later released in tissues needing oxygen. The heme group binds oxygen while still attached to the <scene name='Hemoglobin/Oxysubunit/8'>hemoglobin monomer</scene>. The spacefill view of the hemoglobin polypeptide subunit with an oxygenated heme group shows how the <scene name='Hemoglobin/Oxysubunitsf/4'>oxygenated heme group is held</scene> within the polypeptide.
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[[Tumor Necrosis Factor Receptor]]<br />
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<scene name='Hemoglobin/Anchortrace/5'>Anchoring of the heme</scene> is facilitated by a histidine nitrogen that binds to the iron. A second histidine is near the bound oxygen. The "arms" (propanoate groups) of the heme are hydrophilic and face the surface of the protein while the hydrophobic portions of the heme are buried among the hydrophobic amino acids of the protein.
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==Blood Clots & Thrombic Events==
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[[P2Y12]]<br />
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Perhaps the most well-known disease caused by a mutation in the hemoglobin protein is sickle-cell anemia. It results from a mutation of the sixth residue in the β hemoglobin monomer from <scene name='Hemoglobin/Hemoglobins_1hho/7'>glutamic acid to a valine</scene>. This hemoglobin variant is termed 'hemoglobin S' ([[2hbs]]).
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**Cancer==
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***Growth Factors
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****Epidermal Growth Factor
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*****[[Epidermal Growth Factor]]
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*****[[Epidermal Growth Factor Receptor]]
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****[[Hepatocyte Growth Factor Receptor]]
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****[[Human Epidermal Growth Factor Receptor 2]]
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****Vascular Growth Factor
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*****[[Vascular Endothelial Growth Factor]]
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*****[[Vascular Endothelial Growth Factor Receptor]]
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***Kinases
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****[[Cell Division Cycle 7-Related Protein Kinase]]
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****Mitogen-Activated Proteins
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*****Mitogen-Activated Protein Kinase
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*****Mitogen-Activated Protein Kinase Kinase
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*****Mitogen-Activated Protein Kinase Kinase Kinase
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******[[c-Raf]]
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****[[Phosphatidylinositol 3-Kinase]]
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****[[Tyrosine Kinase]]
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**[[Heat Shock Protein 90]]
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**[[p53]]
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**[[Mammalian Target of Rapamycin]]
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==Compromised Immune System==
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[[Granulocyte-macrophage colony-stimulating factor]]<br />
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==Diabetes & Hypoglycemia==
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[[Peroxisome Proliferator-Activated Receptors]]<br />
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==Digestive Diseases==
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[[Proton Pump]]<br />
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==Hemoglobin subunit binding O<sub>2</sub>==
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==Erectile Dysfunction==
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For hemoglobin, its function as an oxygen-carrier in the blood is fundamentally linked to the equilibrium between the two main states of its quaternary structure, the unliganded "deoxy" or "T state" versus the liganded "oxy" or "R state". The unliganded (deoxy) form is called the "T" (for "tense") state because it contains extra stabilizing interactions between the subunits. In the high-affinity R-state conformation the interactions which oppose oxygen binding and stabilize the tetramer are somewhat weaker or "relaxed". In some organisms this difference is so pronounced that their Hb molecules dissociate into dimers in the oxygenated form. Structural changes that occur during this transition can illuminate how such changes result in important functional properties, such as cooperativity of oxygen binding and allosteric control by pH and anions. Hemoglobin is definitely not a pure two-state system, but the T to R transition provides the major, first-level explanation of its function.
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[[cGMP-Specific Phosphodiesterase Type 5]]<br />
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The hemoglobin molecule (or "Hb") is a tetramer of two α and two β chains, of 141 and 146 residues in human. They are different but homologous, with a "globin fold" structure similar to [[myoglobin]].
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==HIV==
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[[Reverse Transcriptase]]<br />
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Here we see a single <scene name='Hemoglobin/3hhb_chaina_rainbow/4'>α chain</scene> of hemoglobin, starting with an overview of the subunit. The 6 major and 2 short α-helices that make up the structure of a Hb subunit (the "globin fold") are <scene name='Hemoglobin/3hhb_chaina_heliceslabeled/4'>labeled A through H</scene>, which is the traditional naming scheme. For example, the proximal histidine (the tightest protein Fe ligand) is often called <scene name='Hemoglobin/3hhb_chaina_hisf9/5'>His F9</scene>, since it is residue 9 on helix F (it is residue 87 in the human α chain). The helices form an approximately-cylindrical bundle, with the heme and its central Fe atom bound in a <scene name='Hemoglobin/3hhb_chaina_efpocket/4'>hydrophobic pocket between the E and F helices</scene>.
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==Hypercholesterolemia (Elevated Cholesterol)==
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[[HMG-CoA Reductase]]<br />
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==Hypertension & Congestive Heart Failure==
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[[Angiotensin-Converting Enzyme]]<br />
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[[Calcium Channel]]<br />
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==Inflammation & Rheumatoid Arthritis==
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[[Cyclooxygenase]]<br />
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==Schizophrenia, Bipolar Depression, Insomnia, and Anxiety Disorders==
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[[Dopamine Receptor]]<br />
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[[Andrenergic Receptor]]<br />
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[[Histamine Receptor]]<br />
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[[Opioid Receptor]]<br />
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Revision as of 08:59, 17 September 2010

AstraZeneca’s Nexium
AstraZeneca’s Nexium

The following is a list of major phamerceutical compound targets, organized by disease.

Contents

Alzheimer’s Disease

Acetylcholinesterase
Amyloid Beta
Gamma-Secratase
Glutamate receptor (GluA2)

Anemia

Erythropoietin

Asthma and other Pulmonary Disease States

Beta-2-Andrenergic Receptor
Leukotriene Receptor

Autoimmune Diseases

Tumor Necrosis Factor Receptor

Blood Clots & Thrombic Events

P2Y12

Compromised Immune System

Granulocyte-macrophage colony-stimulating factor

Diabetes & Hypoglycemia

Peroxisome Proliferator-Activated Receptors

Digestive Diseases

Proton Pump

Erectile Dysfunction

cGMP-Specific Phosphodiesterase Type 5

HIV

Reverse Transcriptase

Hypercholesterolemia (Elevated Cholesterol)

HMG-CoA Reductase

Hypertension & Congestive Heart Failure

Angiotensin-Converting Enzyme
Calcium Channel

Inflammation & Rheumatoid Arthritis

Cyclooxygenase

Schizophrenia, Bipolar Depression, Insomnia, and Anxiety Disorders

Dopamine Receptor
Andrenergic Receptor
Histamine Receptor
Opioid Receptor

Proteopedia Page Contributors and Editors (what is this?)

David Canner

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