Rebecca Martin/Sandbox1: Difference between revisions

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::Nine antiparrallel beta strands comprise variable or V-regions. Loop sequences of varying length connect the strands. The 9 strands form 2 beta sheets, one with 4 (ABED-prosite) strands and the other with 3 sIgA2(nov 22 2007) <ref name="CFG">(nov 22 2007). "Superfamily: immunoglobulin." SCOP, from http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.c.b.b.html.</ref>. The remaining 2 strands (C’ and C”) lie in between the 2 sheets. A disulfide bride stabilizes the 2 sandwich halves. Hydrophobic residues face the interior of the sheet, providing stability, while hydrophillic residues face outward and interact with the local environment. The extra loops in the V-region are critical for epitope specificity, and are consequently known as the compliment determining regions, here shown on the <scene name='Rebecca_Martin/Sandbox1/Cdr_360_view/2'>Fab molecule</scene>.
::Nine antiparrallel beta strands comprise variable or V-regions. Loop sequences of varying length connect the strands. The 9 strands form 2 beta sheets, one with 4 (ABED-prosite) strands and the other with 3 sIgA2(nov 22 2007) <ref name="CFG">(nov 22 2007). "Superfamily: immunoglobulin." SCOP, from http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.c.b.b.html.</ref>. The remaining 2 strands (C’ and C”) lie in between the 2 sheets. A disulfide bride stabilizes the 2 sandwich halves. Hydrophobic residues face the interior of the sheet, providing stability, while hydrophillic residues face outward and interact with the local environment. The extra loops in the V-region are critical for epitope specificity, and are consequently known as the compliment determining regions, here shown on the <scene name='Rebecca_Martin/Sandbox1/Cdr_360_view/2'>Fab molecule</scene>.
:<scene name='Rebecca_Martin/Sandbox1/Iga1_constant_domain_light/1'>Classic type domain</scene>  
:<scene name='Rebecca_Martin/Sandbox1/Iga1_constant_domain_light/1'>Classic type domain</scene>  
::C-type domains lack the C' and C'' beta strands <ref name="att" />. The sheets are ABED and CFG. Consequently, the sandwich is more tightly packed. In the antibody, the constant domains determine the isotype: IgA, IgD, IgM, IgG, or IgE.
::C-type domains lack the C' and C<nowiki>''</nowiki> beta strands <ref name="att" />. The sheets are ABED and CFG. Consequently, the sandwich is more tightly packed. In the antibody, the constant domains determine the isotype: IgA, IgD, IgM, IgG, or IgE.
:Related structures
:Related structures
::Proteins containing the classic immunoglobulin-like domain are found predominantly in the immune system <ref name="att" />. In fact, the antibody's closest related structires are those that recognize antigen: MHC and TCRs.
::Proteins containing the classic immunoglobulin-like domain are found predominantly in the immune system <ref name="att" />. In fact, the antibody's closest related structires are those that recognize antigen: MHC and TCRs.

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

Rebecca Martin, Jaime Prilusky