1 / 15

Immunoglobulin

Immunoglobulin. Justas Arasimavi čius. Immunoglobulin. Element of adaptive immune mechanism Better known as antibody It recognize the foreign objects How they work (examples) Animation1 Animation2. Structure of immunoglobulin.

odette
Download Presentation

Immunoglobulin

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript


  1. Immunoglobulin Justas Arasimavičius

  2. Immunoglobulin • Element of adaptive immune mechanism • Better known as antibody • It recognize the foreign objects • How they work (examples) • Animation1 • Animation2

  3. Structure of immunoglobulin • Two identical heavy (H) chains and two identical light (L) chains combine to form this Y-shaped antibody molecule

  4. Disulfide bonds • Bonds between two amino acids result of the SH (sulfhydral) group of one amino acid covalently bonding to the SH group of another amino acid • Stronger than hydrogen bonds • Eg. Hair proteins are held together by disulfide bonds

  5. Heavy chains • The heavy chains each have four domains • Variable domains (VH) • Constant domains (CH1,2,3)

  6. Light chain • The light chains are constructed of two domains • Variable (VL) • Constant (CL)

  7. Structure of immunoglobulin • The fragment antigen binding (Fab fragment) • The fragment crystallizable region (Fc region) • Antibodies bind to antigens by reversible, noncovalent interactions, including hydrogen bonds and charge interactions

  8. How variety is maintained • The variable heavy chain is coded combining 3 genes (VH, DH, JH) • The variable light chain is coded combining 2 genes (VL, JL) • Most likely humans produce between 107 and 109 different shaped Fabs

  9. Antibody Fab region • Antibody (Fab) molecular surface, with the PorA antigen superimposed. • The dark colored groove on the surface of the antibody matches precisely the shape of the PorA antigen • Any changes in the sequence of PorA in this region can disrupt antibody binding http://www.bact.wisc.edu/themicrobialworld/neisseria.html

  10. Antigen binding some pictures

  11. Antigen binding some pictures

  12. Structure of immunoglobulin • Functional consequences: • (VH) and (VL) are positioned to stereochemically react with antigen • The stem is good for mediate effector functions

  13. Hinge • Two disulfide bonds in the hinge region unite the two heavy chains • The hinge allows the two antigen-binding Fab regions of each antibody molecule to move

  14. Conclusion • Changes in the antigen binding site conformation are vital for antigen recognition • Herewith the variety of antibody conformation is vital for our health

  15. Reference • http://www.callutheran.edu/Academic_Programs/Departments/BioDev/omm/jmol/ig_div/start.html • http://en.wikipedia.org/ • http://www.path.cam.ac.uk/~mrc7/mikeimages.html • http://www.tulane.edu/~biochem/med/igg.htm • http://www.biology.arizona.edu/IMMUNOLOGY/tutorials/antibody/structure.html • http://student.ccbcmd.edu/courses/bio141/lecguide/unit5/humoral/abystructure/abystructure.html • http://www.mun.ca/biochem/courses/3107/Topics/Antibodies.html • Abul K. Abbas, Andrew H. Lichtman. Basic Immunology Functions and Disorders of the Immune System. Second Edition 2004

More Related