Group:SMART:Tangible Models of Cdc42 Interacting With Intersectin: Difference between revisions

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 Cell signaling is how cells transmit information from the outside environment to inside the cell as well as how cells propagate messages within the cell. Transmembrane receptors at the cell surface detect environmental changes and pass the information on to intracellular signaling proteins. Proteins that make up signaling pathways pass along messages by interacting with each other.
-Cell movement is integral for survival in both bacterial and eukaryotic cells. In eukaryotes, cells move by changing their cytoskeletons to form actin structures like filopodia. _ese structures are formed in response to signals from outside of cells which are relayed throughout the cell using signaling pathways.
+Cell movement is integral for survival in both bacterial and eukaryotic cells. In eukaryotes, cells move by changing their cytoskeletons to form actin structures like filopodia. These structures are formed in response to signals from outside of cells which are relayed throughout the cell using signaling pathways.
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 ='''<font color = 'black'>How Intersectin Activates Cdc42</font>'''=
-<scene name='SMART_Lincoln_2009/Complex_intersectin_and_cdc42/1'>Cdc42/Intersectin Complex</scene>
+<scene name='SMART_Lincoln_2009/Complex_intersectin_and_cdc42/1'>Cdc42/Intersectin Complex.</scene> The orientation of Alanine 59 is the highlight of Cdc42 activation by Intersectin. Alanine 59 causes the displacement of the Mg++ ion which in turn releases GDP from Cdc42’s binding pocket. Cdc42 is then able to accept a new nucleotide, specifically GTP, to become activated.
-The orientation of Alanine 59 is the highlight of Cdc42 activation by Intersectin. Alanine 59 causes the displacement of the Mg++ ion which in turn releases GDP from Cdc42’s binding pocket. Cdc42 is then able to accept a new nucleotide, specifically GTP, to become activated.
 <applet load='2rh1.pdb' size='350' frame='true'  align='left' scene='SMART_Lincoln_2009/Complex_intersectin_and_cdc42/1'/>
--- <scene name='SMART_Lincoln_2009/Cdc42_and_gdp/1'>Cdc42</scene> (yellow) is off when GDP is in its binding pocket. Mg++ is shown in magenta, Alanine 59 in green, Switch 1 in light gold, and Switch 2 in dark orange. Brown depicts the residues interacting with GDP (Lys16 and Cys18).
+) <scene name='SMART_Lincoln_2009/Cdc42_and_gdp/1'>Cdc42</scene> (yellow) is off when GDP is in its binding pocket. Mg++ is shown in magenta, Alanine 59 in green, Switch 1 in light gold, and Switch 2 in dark orange. Brown depicts the residues interacting with GDP (Lys16 and Cys18).
+) <scene name='SMART_Lincoln_2009/Complex_intersectin_and_cdc42/1'>Intersectin</scene>(blue) binds to Cdc42, and its DH domain interacts with the GTPase.
+) Thee interaction causes conformational changes in Switch 1 and Switch 2 of Cdc42. _r35 hydrogen bonds to a residue (Glu1244) of the DH domain of Intersectin. Most important is the noticeable change in the orientation of residue 59 (Ala59). Its sidechain flips into the magnesium-binding pocket, causing the release of the Mg++ ion and in turn the release of GDP from Cdc42.
+) Mg++ and GDP fall off from Cdc42. the nucleotide-binding pocket of Cdc42 is now empty.
+) Because the intracellular ratio of GTP to GDP is high, a GTP molecule (dark green) will float into the binding pocket of Cdc42 and activate it.
--- <scene name='SMART_Lincoln_2009/Complex_intersectin_and_cdc42/1'>Cdc42/Intersectin Complex</scene>Intersectin (blue) binds to Cdc42, and its DH domain interacts with the GTPase.
--- Thee interaction causes conformational changes in Switch 1 and Switch 2 of Cdc42. _r35 hydrogen bonds to a residue (Glu1244) of the DH domain of Intersectin. Most important is the noticeable change in the orientation of residue 59 (Ala59). Its sidechain flips into the magnesium-binding pocket, causing the release of the Mg++ ion and in turn the release of GDP from Cdc42.
--- Mg++ and GDP fall off from Cdc42. the nucleotide-binding pocket of Cdc42 is now empty.
--- Because the intracellular ratio of GTP to GDP is high, a GTP molecule (dark green) will float into the binding pocket of Cdc42 and activate it.
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 ----
-==<font color = 'red'>MSOE Center for BioMolecular Modeling and SMART Teams</font>==
+=<font color = 'red'>MSOE Center for BioMolecular Modeling and SMART Teams</font>=
 [[Image:Center for BioMolecular Modeling Logo.jpg|left|200px]]
 [[Image:Smart Teams photo 5.jpg|right|120px]]
 <font color = 'red'>SMART  Teams (S</font>tudents <font color = 'red'>M</font>odeling <font color = 'red'>A</font> <font color = 'red'>R</font>esearch <font color = 'red'>T</font>opic) is a science outreach program developed by the MSOE Center for BioMolecular Modeling.  In this program, teams of high school students work with a local resarch lab to design and build a physical model of a protein that is being investigated by the lab.  The goal of the SMART Team program is to introduce students to the real world of scince --- as it exists in a local research lab.  The development of this program was supported by grants from the NIH-NCRR SEPA program (Science Education Partnership Award) and an HHMI Precollege Science Education Award.  For more information about this program, visit the CBM web site at [http://www.rpc.msoe.edu/cbm www.rpc.msoe.edu/cbm] .