https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Dannielle+Ryman 2026-09-25T06:09:48Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_2&diff=1631418 2012-12-12T20:39:47Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='400' color='black' frame='true' align='right' caption='Crystal structure of Focal Adhesion Kinase (FAK) kinase domain complex with ADP [[1mp8]]'/&gt;<br /> <br /> <br /> ===Background===<br /> <br /> '''Collagen''' is a structural protein found in abundance in connective tissues along with the breast tumor microenvironment. Collagen I specifically is the most abundant extracellular matix (ECM) protein found in the primary breast tumor, whereas other collagen types such as Collagen IV and III are commonly found in the basement membrane of the tumor microenvironment. During tumor development TACS (tumor associated collagen signaling) occurs. TACS is the process by which the ECM collagen reorganizes and forms complex fibrous bundles facilitating individual and aggregated primary cells to extravasate the primary tumor site and translocate to a secondary site. <br /> <br /> ===Structure===<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak_solution/3'&gt;NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model.&lt;/scene&gt;Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.&lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/2'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> ==3D structures of focal adhesion kinase==<br /> <br /> [[Focal adhesion kinase]]<br /> <br /> <br /> ===References===<br /> 1.<br /> <br /> 2.<br /> <br /> 3.</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_2&diff=1631223 2012-12-12T20:30:23Z

<p>Dannielle Ryman: New page: &lt;applet load=&#039;1MP8&#039; size=&#039;400&#039; color=&#039;black&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Crystal structure of Focal Adhesion Kinase (FAK) kinase domain complex with ADP 1mp8&#039;/&gt; ===Background...</p> <hr /> <div>&lt;applet load='1MP8' size='400' color='black' frame='true' align='right' caption='Crystal structure of Focal Adhesion Kinase (FAK) kinase domain complex with ADP [[1mp8]]'/&gt;<br /> <br /> <br /> ===Background===<br /> <br /> '''Collagen''' is a structural protein found in abundance in connective tissues along with the breast tumor microenvironment. <br /> <br /> ===Structure===<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak_solution/3'&gt;NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model.&lt;/scene&gt;Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.&lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/2'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> ==3D structures of focal adhesion kinase==<br /> <br /> [[Focal adhesion kinase]]<br /> <br /> <br /> ===References===<br /> 1.<br /> <br /> 2.<br /> <br /> 3.</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman&diff=1631162 2012-12-12T19:17:07Z

<p>Dannielle Ryman: </p> <hr /> <div>[[User:Dannielle Ryman/Sandbox 2]]</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Molecular_Playground/FAK&diff=1338532 2011-12-30T19:24:56Z

<p>Dannielle Ryman: </p> <hr /> <div>(FAK) Focal Adhesion Kinase<br /> <br /> &lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak_solution/3'&gt;NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model.&lt;/scene&gt;Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.&lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/2'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Molecular_Playground/FAK&diff=1338529 2011-12-30T19:05:00Z

<p>Dannielle Ryman: </p> <hr /> <div>(FAK) Focal Adhesion Kinase<br /> <br /> &lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.&lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/2'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Molecular_Playground/FAK&diff=1333898 2011-12-26T14:50:11Z

<p>Dannielle Ryman: </p> <hr /> <div>(FAK) Focal Adhesion Kinase<br /> <br /> &lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/2'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333897 2011-12-26T14:44:32Z

<p>Dannielle Ryman: </p> <hr /> <div>(FAK) Focal Adhesion Kinase<br /> <br /> &lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/2'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333896 2011-12-26T14:40:42Z

<p>Dannielle Ryman: </p> <hr /> <div>(FAK) Focal Adhesion Kinase<br /> <br /> &lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=CBI_Molecules&diff=1333023 2011-12-17T00:32:08Z

<p>Dannielle Ryman: </p> <hr /> <div>These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].<br /> Many of the molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground] (see also [[Molecular Playground|Molecular Playground in Proteopedia]]). Follow the links below to read nontechnical descriptions, in Proteopedia, of these molecules.<br /> <br /> UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.<br /> <br /> It's great to build on a previous entry, but you must leave the earlier one intact and make a copy that you improve and mark as new. Later we will retain the new one with a merged author list.<br /> <br /> Fall 2011: New entries are due 12/16/11. Please append the designation (new Fall 2011) to your new entries. <br /> <br /> <br /> ==Molecules==<br /> Bhatia Lab<br /> <br /> : '''[[Molecular Playground/Alginate-Fall2011]]''', Joe White, David Griffin<br /> <br /> : '''[[Molecular Playground/Alginate-Fall2010]]''', Joe White, David Griffin<br /> <br /> : '''[[Molecular Playground/Poly(ethylene glycol)]]''', Erika M. Saffer<br /> <br /> <br /> [http://chamberslab.com/wp/ Chambers Lab]<br /> <br /> : '''[[Molecular Playground/Glutamate Receptor]]''', Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano<br /> <br /> [http://openwetware.org/wiki/Chien Chien Lab]<br /> <br /> : '''[[Molecular Playground/Hexameric ClpX]]''', Joanne Lau <br /> :: Best CBI Molecule 2011<br /> <br /> Forbes Lab<br /> <br /> <br /> : '''[[Molecular Playground/CheR]]''', Miaomin Zhang<br /> <br /> : '''[[Molecular Playground/RBP]]''', Jan Panteli<br /> <br /> : '''[[Molecular Playground/TRAIL]]''', Charley Swofford<br /> <br /> <br /> [http://www.biochem.umass.edu/garman/index.html Garman Lab]<br /> <br /> : '''[[Molecular Playground/Human Protective Protein Cathepsin A]]''', Yadilette Rivera-Colon<br /> <br /> : '''[[Molecular Playground/Human PPCA]]''', Nilima Kolli<br /> <br /> [http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]<br /> <br /> : '''[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]''', Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy<br /> :: Best Overall CBI Molecule 2010<br /> <br /> : NEW Fall 2011! '''[[Molecular_Playground/DHFR]]''', Karan Hingorani <br /> <br /> [http://people.chem.umass.edu/jhardy/ Hardy Lab]<br /> <br /> : '''[[Molecular Playground/Caspase-7 Dynamics]]'''<br /> <br /> : '''[[Molecular Playground/Caspase-9 Regulation]]''', Kristen Huber<br /> <br /> : '''[[Molecular Playground/Caspase-6 (new)]]''', Elih Velazquez<br /> <br /> : '''[[Molecular Playground/Influenza A M2 transmembrane domain]]''', Samantha Nicholls<br /> <br /> : '''[[Molecular Playground/Dengue Virus Protease]]''', Muslum Yildiz<br /> <br /> Hebert Lab<br /> <br /> : '''[[Molecular Playground/Saposin C]]''', Abla Tannous<br /> : '''[[Molecular_Playground/ERMan1]]''', Johan Sunryd<br /> <br /> <br /> [http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]<br /> <br /> : '''[[Molecular_Playground/Pcr H]]''', Fabian Romano<br /> <br /> [http://www.chem.umass.edu/people/kaltashovlab/ Kaltashov Lab]<br /> <br /> : '''[[Molecular Playground/Velaglucerase]]''', Adriana Kita <br /> <br /> <br /> <br /> Knapp lab<br /> <br /> :'''[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]''', Cristina Martin<br /> :: Best CBI Molecule Proteopedia Page 2010<br /> <br /> : '''[[Molecular Playground/FIH]]''', Cornelius Taabazuing, Breanne Holmes, John Hangasky<br /> <br /> [http://www.chem.umass.edu/~cmartin/ Martin Lab]<br /> <br /> : '''[[Molecular Playground/T7 RNAP Conformations]]''', Luis E. Ramirez-Tapia <br /> :: Best CBI Molecule 2011<br /> : '''[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]''', Ankit Vahia<br /> <br /> : NEW Fall 2011! '''[[Molecular Playground/Human mtRNA pol]]''', Ketan Mathavan <br /> <br /> Peyton Lab<br /> : NEW FALL 2011! '''[[Molecular Playground/C-Raf]]''', Thuy Nguyen<br /> : NEW FALL 2011! '''[[Molecular Playground/FAK]]''', Dannielle Ryman<br /> <br /> <br /> <br /> [http://roberts.openwetware.org/ Roberts Lab]<br /> <br /> : '''[[Molecular Playground/Taxol]]''', Rohan Patil, Sarah Wilson<br /> <br /> : '''[[Molecular Playground/Insulin]]''', Whitney Stoppel<br /> <br /> [http://www.umass.edu/rotellogroup/ Rotello Lab]<br /> <br /> : '''[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]''', Daniel Moyano-Marino<br /> <br /> : '''[[Molecular Playground/Pancreatic Lipase]]''', Rui Tang<br /> <br /> : '''[[Molecular playground/Chymotrypsin]]''', Brad<br /> <br /> : '''[[Molecular Playground/Targeting Peptide]]''', David Solfiell<br /> <br /> Schnarr Lab <br /> <br /> : '''[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]''', Tsung-Yi Lin, Jon Amoroso<br /> <br /> : '''[[Molecular Playground/ACP apo]]''', Gitanjeli Prasad<br /> <br /> Tew Lab<br /> <br /> : NEW FALL 2011!! '''[http://www.proteopedia.com/wiki/index.php/Molecular_Playground/HIV_Tat Molecular Playground/HIV Tat]''', Brittany deRonde<br /> <br /> <br /> Thayumanavan Lab<br /> <br /> : '''[[Molecular Playground/Lysozyme ]]''', Daniella Gonzalez<br /> <br /> : '''[[Molecular Playground/Beta-galactosidase]]''', Judy Ventura<br /> <br /> : '''[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]''', Krishna Reddy Raghupathi<br /> <br /> : '''[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]''', Rami Rajasekar Reddy<br /> <br /> : '''[[Molecular Playground/Biotin binding avidin]]''', Diego Amado <br /> <br /> : '''[[User:Jiaming Zhuang|Molecular Playground/MMP12]]''', Jiaming Zhuang<br /> <br /> : ''' [[User:Jing Guo|Molecular Playground/Gluconase]]''', Jing Guo<br /> <br /> : '''[[Molecular Playground/Glutathione Reductase]]''', Reuben Chacko<br /> <br /> Thayumanavan &amp; Vachet Labs<br /> <br /> : '''[[Molecular Playground/Trypsin]]''', Gladys Murage<br /> <br /> [http://people.chem.umass.edu/thompson/index.html Thompson] &amp; [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs<br /> <br /> : '''[[Molecular Playground/Bacterial Chemotaxis Receptors]]''', Lynmarie K. Thompson, Shiela M. Jones<br /> <br /> : '''[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]''', Meili Yang<br /> <br /> : New Fall 2011 '''[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]''', Xuni Li<br /> <br /> <br /> [http://www.chem.umass.edu/~vachet/index.html Vachet Lab]<br /> <br /> : '''[[Molecular playground/beta 2 microglobulin]]''', Nick Borotto<br /> :: Best CBI Molecule Jmol scenes 2010<br /> <br /> : '''[[Molecular Playground/Myoglobin]]''', Yuping Zhou <br /> <br /> :'''[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]''', Shaynah Browne<br /> <br /> <br /> <br /> Other Molecules of interest<br /> <br /> : '''[[Molecular Playground/PcrA Helicase]]''', Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]<br /> <br /> <br /> Other Laboratories<br /> <br /> : '''[[Molecular Playground/YKL-40]]''', Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]<br /> <br /> : '''[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]''', Daniel Seeman, Dubin Lab<br /> <br /> : '''[[Molecular Playground/ADAM13]]''', Genevieve Abbruzzese, Alfandari Lab<br /> <br /> ==Instructions==<br /> <br /> '''Congratulations to the prize-winning CBI molecules noted above! These also provide great examples to follow. Another prize for best CBI Molecule page and/or scene will be awarded in summer 2012!'''<br /> <br /> Fall 2011: Complete steps 1-4 by 12/1/11, in preparation for the CBI Molecule Workshop.<br /> <br /> Choose a molecule that is part of your research project. If someone in your group has already made a page for your research molecule, you can improve on that previous entry. You must leave the previously created page intact and make a copy that you improve and mark as new. Later we will retain the new one with a merged author list.<br /> <br /> 1. If you don't already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.<br /> <br /> 2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description (Enter &quot;User:Your Name/Sandbox 1&quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). <br /> <br /> 3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.<br /> <br /> 4. Add a link to your sandbox page at [[Sandbox_CBI]] (CBI Molecules in Progress).<br /> <br /> 5. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.<br /> <br /> 6. Choose a &quot;green scene&quot; on your Proteopedia page to suggest for display at the Molecular Playground and specify a &quot;banner&quot; which will be projected with the molecule. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: &quot;Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to &quot;smell&quot; their environment.&quot;<br /> <br /> 7. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &quot;Molecular Playground/your molecule&quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.<br /> <br /> 8. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the examples above, and be sure to mark it as NEW FALL 2011. If you are improving a previously created page, leave the old one intact and make a copy that you improve and mark as new. Later we will retain the new one with a merged author list. When multiple authors contribute to a Molecular Playground page, please indicate your scene with your initials. Please link the lab names to web pages too.<br /> <br /> ==Links to HELP pages==<br /> Videos showing how to use Proteopedia:<br /> [[Proteopedia:Video_Guide]]<br /> (Sometimes slow -- if you pause the video and wait awhile it will download and then you can play it without interruptions)<br /> <br /> [[Proteopedia:DIY:Scenes|Proteopedia Scenes: Do It Yourself]]<br /> gives succinct step by step instructions on how to create a molecular scene.<br /> <br /> A powerpoint-like set of slides that walks a user through the process of creating a new page and a new molecular scene/green link.<br /> [http://www.proteopedia.org/wiki/images/1/1b/2009_07_13_Proteopedia_Workshop.pdf Proteopedia Workshop Slides]<br /> <br /> [[Proteopedia:Guidelines for Ethical Writing]].<br /> Please pay attention to the section about images. There are links to examples of images re-used with explicit permission.<br /> <br /> For other help resources, click on [[Help:Contents|Help]] in the ''navigation'' box at the upper left of every page in Proteopedia.</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Molecular_Playground/FAK&diff=1333022 2011-12-17T00:28:13Z

<p>Dannielle Ryman: New page: (FAK) Focal Adhesion Kinase &lt;applet load=&#039;1MP8&#039; size=&#039;300&#039; color=&#039;black&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;FAK)Crystal structure of Focal Adhesion Kinase (FAK)&#039;&#039;/&gt; &lt;applet load=&#039;2IJM&#039; ...</p> <hr /> <div>(FAK) Focal Adhesion Kinase<br /> <br /> &lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> [[Image:Nrm2996-f3.jpg |thumb|left|450x200px|]]<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|right|450x200px|]]<br /> <br /> <br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Sandbox_CBI&diff=1333021 2011-12-17T00:23:54Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;!-- <br /> Please use the &quot;3D&quot; button above this box to insert a Jmol applet (molecule) on this page.<br /> Or use the four-green-boxes-button to insert scrollable text adjacent<br /> to a Jmol applet. Check out the other buttons as well! <br /> --&gt;<br /> <br /> This page is for links to CBI Molecules in Progress (user sandbox pages).<br /> <br /> <br /> <br /> http://proteopedia.org/wiki/index.php/Ketan_Mathavan/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Brittany_deRonde/Sandbox_1<br /> <br /> <br /> http://proteopedia.org/wiki/index.php/Heidi_Hu/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/User:Xuni_Li/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Gustavo_Elberto_Epalza_Sanchez/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Scott_Eron/Sandbox_1<br /> <br /> http://www.proteopedia.org/wiki/index.php/User:Jing_Liu/Sandbox_1<br /> <br /> http://www.proteopedia.com/wiki/index.php/User:Karan_Hingorani/sandbox_2</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Sandbox_CBI&diff=1333010 2011-12-16T23:41:24Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;!-- <br /> Please use the &quot;3D&quot; button above this box to insert a Jmol applet (molecule) on this page.<br /> Or use the four-green-boxes-button to insert scrollable text adjacent<br /> to a Jmol applet. Check out the other buttons as well! <br /> --&gt;<br /> <br /> This page is for links to CBI Molecules in Progress (user sandbox pages).<br /> <br /> http://proteopedia.org/wiki/index.php/User:Dannielle_Ryman/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Ketan_Mathavan/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Brittany_deRonde/Sandbox_1<br /> <br /> <br /> http://proteopedia.org/wiki/index.php/Heidi_Hu/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/User:Xuni_Li/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Gustavo_Elberto_Epalza_Sanchez/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Scott_Eron/Sandbox_1<br /> <br /> http://www.proteopedia.org/wiki/index.php/User:Jing_Liu/Sandbox_1<br /> <br /> http://www.proteopedia.com/wiki/index.php/User:Karan_Hingorani/sandbox_2</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333009 2011-12-16T23:33:52Z

<p>Dannielle Ryman: </p> <hr /> <div>(FAK) Focal Adhesion Kinase<br /> <br /> &lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> [[Image:Nrm2996-f3.jpg |thumb|left|450x200px|]]<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|right|450x200px|]]<br /> <br /> <br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Sandbox_CBI&diff=1333007 2011-12-16T23:29:23Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;!-- <br /> Please use the &quot;3D&quot; button above this box to insert a Jmol applet (molecule) on this page.<br /> Or use the four-green-boxes-button to insert scrollable text adjacent<br /> to a Jmol applet. Check out the other buttons as well! <br /> --&gt;<br /> <br /> This page is for links to CBI Molecules in Progress (user sandbox pages).<br /> <br /> http://proteopedia.org/wiki/index.php/Ketan_Mathavan/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Brittany_deRonde/Sandbox_1<br /> <br /> <br /> http://proteopedia.org/wiki/index.php/Heidi_Hu/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/User:Xuni_Li/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Gustavo_Elberto_Epalza_Sanchez/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Scott_Eron/Sandbox_1<br /> <br /> http://www.proteopedia.org/wiki/index.php/User:Jing_Liu/Sandbox_1<br /> <br /> http://www.proteopedia.com/wiki/index.php/User:Karan_Hingorani/sandbox_2</div>

Dannielle Ryman https://proteopedia.org/index.php?title=Sandbox_CBI&diff=1333006 2011-12-16T23:28:24Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;!-- <br /> Please use the &quot;3D&quot; button above this box to insert a Jmol applet (molecule) on this page.<br /> Or use the four-green-boxes-button to insert scrollable text adjacent<br /> to a Jmol applet. Check out the other buttons as well! <br /> --&gt;<br /> <br /> This page is for links to CBI Molecules in Progress (user sandbox pages).<br /> <br /> http://proteopedia.org/wiki/index.php/User:Dannielle_Ryman/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Ketan_Mathavan/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Brittany_deRonde/Sandbox_1<br /> <br /> <br /> http://proteopedia.org/wiki/index.php/Heidi_Hu/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/User:Xuni_Li/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Gustavo_Elberto_Epalza_Sanchez/Sandbox_1<br /> <br /> http://proteopedia.org/wiki/index.php/Scott_Eron/Sandbox_1<br /> <br /> http://www.proteopedia.org/wiki/index.php/User:Jing_Liu/Sandbox_1<br /> <br /> http://www.proteopedia.com/wiki/index.php/User:Karan_Hingorani/sandbox_2</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333005 2011-12-16T23:23:38Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> [[Image:Nrm2996-f3.jpg |thumb|left|450x200px|]]<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|right|450x200px|]]<br /> <br /> <br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333004 2011-12-16T23:14:27Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> <br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> <br /> ===Background===<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> [[Image:Nrm2996-f3.jpg |thumb|left|450x200px|]]<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333003 2011-12-16T23:12:43Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='(FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> [[Image:Nrm2996-f3.jpg |thumb|left|450x200px|]]<br /> <br /> Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333002 2011-12-16T23:11:53Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='(FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm2996-f3.jpg |thumb|left|650x400px|]]Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|left|650x400px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1333001 2011-12-16T23:10:51Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='(FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm2996-f3.jpg |thumb|left|450x200px|]]Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332998 2011-12-16T23:08:32Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='(FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:nrm2996-f3.jpg|thumb|left|450x200px|]]Focal adhesion kinase (FAK) activation by phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2)-induced conformational change. In the inactive state, FAK adopts a closed, auto-inhibited conformation through interactions between its four-point-one, ezrin, radixin, moesin (FERM) and kinase domains. <br /> <br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005<br /> <br /> 3. Margaret C. Frame. Nature Reviews, 2010</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332997 2011-12-16T23:01:01Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;applet load='1MP8' size='300' color='black' frame='true' align='right' caption='(FAK)Crystal structure of Focal Adhesion Kinase (FAK)''/&gt;<br /> &lt;applet load='2IJM' size='300' color='black' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP''/&gt;<br /> <br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332996 2011-12-16T22:56:22Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='300' frame='true' align='right' caption='Crystal structure of Focal Adhesion Kinase (FAK)' scene='Crystal structure of Focal Adhesion Kinase (FAK)'/&gt;<br /> <br /> &lt;Structure load='2ijm' size='300' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP' scene='FAK Domain'/&gt;<br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332995 2011-12-16T22:55:37Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Crystal structure of Focal Adhesion Kinase (FAK)' scene='Crystal structure of Focal Adhesion Kinase (FAK)'/&gt;<br /> <br /> &lt;Structure load='2ijm' size='250' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP' scene='FAK Domain'/&gt;<br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> <br /> 2. Satyajit K. Mitra. Nature Reviews, 2005</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332994 2011-12-16T22:51:08Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Crystal structure of Focal Adhesion Kinase (FAK)' scene='Crystal structure of Focal Adhesion Kinase (FAK)' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;FAK Focal Adhesion Kinase&lt;/scene&gt;<br /> <br /> &lt;Structure load='2ijm' size='250' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP' scene='FAK Domain'/&gt;<br /> <br /> ===Background===<br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> 2. Satyajit K. Mitra. Nature Reviews, 2005</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332993 2011-12-16T22:50:04Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Crystal structure of Focal Adhesion Kinase (FAK)' scene='Crystal structure of Focal Adhesion Kinase (FAK)' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;FAK Focal Adhesion Kinase&lt;/scene&gt;<br /> <br /> &lt;Structure load='2ijm' size='250' frame='true' align='right' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP' scene='FAK Domain'/&gt;<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> 2. Satyajit K. Mitra. Nature Reviews, 2005</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332992 2011-12-16T22:49:13Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Crystal structure of Focal Adhesion Kinase (FAK)' scene='Crystal structure of Focal Adhesion Kinase (FAK)' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;FAK Focal Adhesion Kinase&lt;/scene&gt;<br /> <br /> &lt;Structure load='2ijm' size='500' frame='true' align='left' caption='Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP' scene='FAK Domain'/&gt;<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> 2. Satyajit K. Mitra. Nature Reviews, 2005</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332991 2011-12-16T22:39:31Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;FAK Focal Adhesion Kinase&lt;/scene&gt;<br /> <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/1'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:Nrm1549-f2.jpg|thumb|left|450x200px|]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001<br /> 2. Satyajit K. Mitra. Nature Reviews, 2005</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332989 2011-12-16T22:32:28Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;FAK Focal Adhesion Kinase&lt;/scene&gt;<br /> <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/1'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> [[Image:http://www.nature.com/nrm/journal/v6/n1/images/nrm1549-f2.jpg]]<br /> Focal adhesion kinase (FAK) contains a FERM (protein 4.1, ezrin, radixin and moesin homology) domain, a kinase domain and a focal adhesion targeting (FAT) domain. The FERM domain mediates interactions of FAK with the epidermal growth factor (EGF) receptor, platelet-derived growth factor (PDGF) receptor, the ETK tyrosine kinase and ezrin, and the FERM domain can be conjugated to SUMO (small ubiquitin-related modifier) at Lys152. The FAT domain recruits FAK to focal contacts by associating with integrin-associated proteins such as talin and paxillin. It also links FAK to the activation of Rho GTPases by binding to guanine nucleotide-exchange factors (GEFs) such as p190 RhoGEF. FAK contains three proline-rich regions (PRR1–3), which bind Src-homology-3 (SH3) domain-containing proteins such as p130Cas, the GTPase regulator associated with FAK (GRAF) and the Arf-GTPase-activating protein ASAP1. FAK is phosphorylated (P) on several tyrosine residues, including Tyr397, 407, 576, 577, 861 and 925. Tyrosine phosphorylation on Tyr397 creates a Src-homology-2 (SH2) binding site for Src, phospholipase Cgamma (PLCgamma), suppressor of cytokine signalling (SOCS), growth-factor-receptor-bound protein 7 (GRB7), the Shc adaptor protein, p120 RasGAP and the p85 subunit of phosphatidylinositol 3-kinase (PI3K). Phosphorylation of Tyr576 and Tyr577 within the kinase domain is required for maximal FAK catalytic activity, whereas the binding of FAK-family interacting protein of 200 kDa (FIP200) to the kinase region inhibits FAK catalytic activity. FAK phosphorylation at Tyr925 creates a binding site for GRB2.<br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332988 2011-12-16T22:26:38Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;FAK Focal Adhesion Kinase&lt;/scene&gt;<br /> <br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak2/1'&gt;Crystal Structure of Focal Adhesion Kinase Domain with 2 molecules in the Asymmetric Unit Complexed with ADP and ATP&lt;/scene&gt;<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. <br /> <br /> ===Structure===<br /> <br /> <br /> <br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics, 2001</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1332986 2011-12-16T22:11:52Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> Focal adhesion kinase (FAK) is a protein tyrosine kinase which is recruited at an early stage to focal adhesions and which mediates many of the downstream responses. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis.<br /> <br /> ===Structure===<br /> <br /> <br /> ===Catalysis===<br /> <br /> <br /> <br /> <br /> ===Drug Target===<br /> <br /> <br /> <br /> <br /> <br /> <br /> <br /> ===References===<br /> 1. Noble, Molecular Biophysics</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1329686 2011-12-07T18:06:57Z

<p>Dannielle Ryman: </p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> &lt;scene name='User:Dannielle_Ryman/Sandbox_1/Fak/1'&gt;TextToBeDisplayed&lt;/scene&gt;</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman/Sandbox_1&diff=1329671 2011-12-07T18:02:12Z

<p>Dannielle Ryman: New page: &lt;Structure load=&#039;1MP8&#039; size=&#039;500&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Insert caption here&#039; scene=&#039;Insert optional scene name here&#039; /&gt;</p> <hr /> <div>&lt;Structure load='1MP8' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;</div>

Dannielle Ryman https://proteopedia.org/index.php?title=User:Dannielle_Ryman&diff=1329668 2011-12-07T18:01:34Z

<p>Dannielle Ryman: </p> <hr /> <div>[[User:Dannielle Ryman/Sandbox 1]]</div>

Dannielle Ryman