User:Susan Corradino

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(Introduction)
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== Introduction ==
== Introduction ==
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Calnexin is an [http://academic.brooklyn.cuny.edu/biology/bio4fv/page/integra.htm integral protein] found in the plasma membrane of the endoplasmic reticulum. This protein functions as a [http://youtu.be/b39698t750c chaperone protein] , forming a super-complex which aids in the formation of the MHC complex. The MHC complex comes in two forms, [http://www.ncbi.nlm.nih.gov/books/NBK27098/figure/A361/?report=objectonly MHC class I] and MHC class II. This molecule is responsible for peptide presentation to T cells in the adaptive immune response. MHC I complex forms and matures in the endoplasmic reticulum of the cell. Once the peptide is bound to the heavy chain of the peptide binding cleft, the molecule will migrate out of the endoplasmic reticulum to the cytosol eventually making its way to the cell surface for presentation to T lymphocytes. T cells will [http://www.ncbi.nlm.nih.gov/books/NBK27098/figure/A372/?report=objectonly bind] to the MHC I complex when antigen recognition has occurred. Without calnexin, the MHC complex would be compromised and ultimately be unable to present the peptide required for the immune response. An interesting additional function of the protein is to ensure that misfolded glycoproteins remain in the ER until they are disposed of by the appropriate regulating structures. Calnexin has also been described as a player in aiding in the proper folding of polypeptides
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Calnexin is an [http://academic.brooklyn.cuny.edu/biology/bio4fv/page/integra.htm integral protein] found in the plasma membrane of the endoplasmic reticulum. This protein functions as a [http://youtu.be/b39698t750c chaperone protein] , forming a super-complex which aids in the formation of the MHC complex. The MHC complex comes in two forms, [http://www.ncbi.nlm.nih.gov/books/NBK27098/figure/A361/?report=objectonly MHC class I] and MHC class II. This molecule is responsible for peptide presentation to T cells in the adaptive immune response. MHC I complex forms and matures in the endoplasmic reticulum of the cell. Once the peptide is bound to the heavy chain of the peptide binding cleft, the molecule will migrate out of the endoplasmic reticulum to the cytosol eventually making its way to the cell surface for presentation to T lymphocytes. T cells will [http://www.ncbi.nlm.nih.gov/books/NBK27098/figure/A372/?report=objectonly bind] to the MHC I complex when antigen recognition has occurred (Janeway 2001). Without calnexin, the MHC complex would be compromised and ultimately be unable to present the peptide required for the immune response. An interesting additional function of the protein is to ensure that misfolded glycoproteins remain in the ER until they are disposed of by the appropriate regulating structures. Calnexin has also been described as a player in aiding in the proper folding of polypeptides
== 3D Structure ==
== 3D Structure ==
This molecule is asymmetrical in shape with two unique domains. The long protruding arm of the protein is thought to function with the communication between calnexin and other proteins, specifically ERp57, a secondary chaperon protein in the formation of the [http://youtu.be/vrFMWyJwGxw MHC I complex], this section of the protein gives the protein a unique crystal structure that is unlike other proteins (Schrag et al 2001). This arm also provides the contact point for all intermolecular communication (Schrag et al 2001). There are two significant disulfide bonds found in the long arm of calnexin, <scene name='User:Susan_Corradino/Cys161longarm/1'>Cys161</scene>-<scene name='User:Susan_Corradino/Cys195longarm/1'>Cys195</scene> and Cys361-Cys367 (Schrag et al 2001). Important amino acids in this section of the crystal structure of calnexin include Lys135 and residues of 173-178 found in the lectin domain as well as Trp343 and residues 346-349. This aspect of the crystal structure will allow the arm of the molecule to wrap around associate proteins to form the super complex for the MHC I (Schrag et al 2001).The second domain which is globular lectin in nature provides the ability to [http://bit.ly/GOBMjE monovalently] bind [http://bit.ly/GWZFGP glycan].
This molecule is asymmetrical in shape with two unique domains. The long protruding arm of the protein is thought to function with the communication between calnexin and other proteins, specifically ERp57, a secondary chaperon protein in the formation of the [http://youtu.be/vrFMWyJwGxw MHC I complex], this section of the protein gives the protein a unique crystal structure that is unlike other proteins (Schrag et al 2001). This arm also provides the contact point for all intermolecular communication (Schrag et al 2001). There are two significant disulfide bonds found in the long arm of calnexin, <scene name='User:Susan_Corradino/Cys161longarm/1'>Cys161</scene>-<scene name='User:Susan_Corradino/Cys195longarm/1'>Cys195</scene> and Cys361-Cys367 (Schrag et al 2001). Important amino acids in this section of the crystal structure of calnexin include Lys135 and residues of 173-178 found in the lectin domain as well as Trp343 and residues 346-349. This aspect of the crystal structure will allow the arm of the molecule to wrap around associate proteins to form the super complex for the MHC I (Schrag et al 2001).The second domain which is globular lectin in nature provides the ability to [http://bit.ly/GOBMjE monovalently] bind [http://bit.ly/GWZFGP glycan].

Revision as of 11:39, 5 April 2012

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*Susan Corradino
  • Graduate student
  • State University of New York, Old Westbury
  • Old Westbury, NY, USA
  • Education (Biology). B.S. Marine Vertebrate Biology.


Introduction

Calnexin is an integral protein found in the plasma membrane of the endoplasmic reticulum. This protein functions as a chaperone protein , forming a super-complex which aids in the formation of the MHC complex. The MHC complex comes in two forms, MHC class I and MHC class II. This molecule is responsible for peptide presentation to T cells in the adaptive immune response. MHC I complex forms and matures in the endoplasmic reticulum of the cell. Once the peptide is bound to the heavy chain of the peptide binding cleft, the molecule will migrate out of the endoplasmic reticulum to the cytosol eventually making its way to the cell surface for presentation to T lymphocytes. T cells will bind to the MHC I complex when antigen recognition has occurred (Janeway 2001). Without calnexin, the MHC complex would be compromised and ultimately be unable to present the peptide required for the immune response. An interesting additional function of the protein is to ensure that misfolded glycoproteins remain in the ER until they are disposed of by the appropriate regulating structures. Calnexin has also been described as a player in aiding in the proper folding of polypeptides

3D Structure

This molecule is asymmetrical in shape with two unique domains. The long protruding arm of the protein is thought to function with the communication between calnexin and other proteins, specifically ERp57, a secondary chaperon protein in the formation of the MHC I complex, this section of the protein gives the protein a unique crystal structure that is unlike other proteins (Schrag et al 2001). This arm also provides the contact point for all intermolecular communication (Schrag et al 2001). There are two significant disulfide bonds found in the long arm of calnexin, - and Cys361-Cys367 (Schrag et al 2001). Important amino acids in this section of the crystal structure of calnexin include Lys135 and residues of 173-178 found in the lectin domain as well as Trp343 and residues 346-349. This aspect of the crystal structure will allow the arm of the molecule to wrap around associate proteins to form the super complex for the MHC I (Schrag et al 2001).The second domain which is globular lectin in nature provides the ability to monovalently bind glycan.

Proteopedia Page Contributors and Editors (what is this?)

Susan Corradino, Eric Martz

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