Sandbox GGC1: Difference between revisions

Latest revision as of 22:13, 28 April 2021

Kinesin Motor DomainKinesin Motor Domain

Kinesin is an ATP-dependent motor protein responsible for the transportation of cargo. It is a heterotetramer composed of light and heavy chains.

Function

Moving cargo usually from the center of the cell to the margins
Involved in cell replication and axonal signaling

Disease

Charcot Marie Tooth (CMT): Charcot Marie Tooth is one of many diseases that affect the peripheral nervous system. Individuals may suffer physical disabilities due to weakness in transmission of signals firing from the central nervous system

Structural highlights

Scene #1: Kinesin structure is composed of eight anti-parallel Beta sheets and three alpha helices on opposite sides

Scene #2: This is the ATP binding site. Upon the binding of phosphate to ADP, ATP is formed giving Kinesin the energy needed to move the cargo one step a head to its destination

Scene #3: This is the Microtubule-binding site, where Kinesin binds to microtubules for stability

Scene #4: some patients with CMT show mutation in the p-loop. A missense mutation results in a leucine in place of glutamine affecting signal transmission

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

ReferencesReferences

file:///C:/Users/Muna/Desktop/Spring%202021/Advanced%20Biochem/pcbi.1003329.pdf
https://www.ncbi.nlm.nih.gov/books/NBK22572/#:~:text=Kinesins%20moving%20along%20microtubules%20usually,surfaces%20of%20some%20eukaryotic%20cells.
https://www.ninds.nih.gov/Disorders/Patient-Caregiver-Education/Fact-Sheets/Charcot-Marie-Tooth-Disease-Fact-Sheet

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

James Nolan, Jackie Ha., Student

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-== Chymotrypsin ==
+==Kinesin Motor Domain==
-<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
+<StructureSection load='1bg2' size='340' side='right' caption='Kinesin Protein' scene=''>
-<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>
+Kinesin is an ATP-dependent motor protein responsible for the transportation of cargo. It is a heterotetramer composed of light and heavy chains.
-== Structural Highlights and Function ==
+== '''Function''' ==
-Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
+* Moving cargo usually from the center of the cell to the margins <br/>
-The S1 binding pocket is responsible for stabilizing the substrate before cleaving. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine.
+* Involved in cell replication and axonal signaling
-Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow.
-The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of a monomer is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.
+== '''Disease''' ==
+*Charcot Marie Tooth (CMT): Charcot Marie Tooth is one of many diseases that affect the peripheral nervous system. Individuals may suffer physical disabilities due to weakness in transmission of signals firing from the central nervous system
+== '''Structural highlights''' ==
+;Scene #1: Kinesin structure is composed of eight anti-parallel Beta sheets and three alpha helices on opposite sides <scene name='75/752263/Alpha_beta_sheets/5'> Alpha-beta structure </scene>
+;Scene #2: This is the ATP binding site. Upon the binding of phosphate to ADP, ATP is formed giving Kinesin the energy needed to move the cargo one step a head to its destination <scene name='75/752263/Atp_binding_site/5'> ATP-binding site </scene>
+;Scene #3: This is the Microtubule-binding site, where Kinesin binds to microtubules for stability <scene name='75/752263/Mt-binding_site/1'> MT-binding site </scene>
+;Scene #4: some patients with CMT show mutation in the p-loop. A missense mutation results in a leucine in place of glutamine affecting signal transmission <scene name='75/752263/Cmt/1'> CMT </scene>
+This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 </StructureSection>
 == References ==
+#file:///C:/Users/Muna/Desktop/Spring%202021/Advanced%20Biochem/pcbi.1003329.pdf
+#https://www.ncbi.nlm.nih.gov/books/NBK22572/#:~:text=Kinesins%20moving%20along%20microtubules%20usually,surfaces%20of%20some%20eukaryotic%20cells.
+#https://www.ninds.nih.gov/Disorders/Patient-Caregiver-Education/Fact-Sheets/Charcot-Marie-Tooth-Disease-Fact-Sheet
 <references/>