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C-Cadherin Ectodomain Structure and Implications for Cell Adhesion Mechanisms

C-Cadherin Ectodomain Structure and Implications for Cell Adhesion Mechanisms. Titus J. Boggon, John Murray, Sophie Chappuis-Flament, Ellen Wong, Barry M. Gumbiner,Lawrence Shapiro Science 296, 1308-1313(2002). PDB ID:1L3W. 姓名： 嚴家俊 學號： M93360020. Titus J. Boggon, John Murray, 1,4

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C-Cadherin Ectodomain Structure and Implications for Cell Adhesion Mechanisms

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  1. C-Cadherin Ectodomain Structure and Implications for Cell Adhesion Mechanisms Titus J. Boggon, John Murray, Sophie Chappuis-Flament, Ellen Wong, Barry M. Gumbiner,Lawrence Shapiro Science 296, 1308-1313(2002) PDB ID:1L3W 姓名：嚴家俊 學號：M93360020

  2. Titus J. Boggon, John Murray,1,4 Sophie Chappuis-Flament,Ellen Wong, Barry M. Gumbiner,5 Lawrence Shapiro1,2,3,4 1Departments of Biochemistry and Molecular Biophysics,2Department of Ophthalmology, 3NaomiBerrie Diabetes Center, Columbia University College of Physicians and Surgeons, 630 West 168th Street,New York, NY 10032, USA. 4Structural Biology Program,Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029, USA. 5Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center,New York, NY 10021, USA.

  3. Molecular Biology of the Cell. 4th ed.

  4. Each interdomain boundary by 3 Ca+2 ions

  5. Ectodomain 5 two disulfide bonds(Cys448-Cys532 Cys530-Cys539)

  6. Glycosylation sites Red:O-linked Blue:N-linked

  7. Paper`s main question • How could C-cadherin form strand dimer? • How could C-cadherin form cis dimer?

  8. We can analyze • Which amino acids interaction with Ca+2? • Which amino acids has been glycosylation and how these glycosylated sites interaction with C-cadherin domain? • Which amino acid sequences are conserved and what are these sequences function?

  9. Ca+2 interaction with interdomain amino acids

  10. EC1-EC2 ineraction eith Ca+2600 ASN102 ASN104 ASP134 ASP136 ASN143 ASP195

  11. EC1-EC2 ineraction eith Ca+2601 GLU11 GLU69 ASP100 GLN101 ASP103 ASP136

  12. EC1-EC2 ineraction eith Ca+2602 GLU11 ASP67 GLU69 ASP103

  13. EC2-EC3 ineraction eith Ca+2603 GLU119 GLU182 ASP213 ALA214 ASP216 ASP248

  14. EC2-EC3 ineraction eith Ca+2604 GLU119 ASP180 GLU182 ASP216

  15. EC2-EC3 ineraction eith Ca+2605 ASN215 ASN217 ASP246 ASP248 ALA254 ASN304

  16. EC3-EC4 ineraction eith Ca+2606 GLU232 ASP289 GLU291 GLU328

  17. EC3-EC4 ineraction eith Ca+2607 ASN327 GLU328 ASP358 ASP360 GLN365 ASP414

  18. EC3-EC4 ineraction eith Ca+2610 GLU291 ASP325 VAL326 GLU328 ASP360

  19. EC4-EC5 ineraction eith Ca+2608 GLU343 ASP395 GLU397 ASP435

  20. EC4-EC5 ineraction eith Ca+2609 ASN434 ASN436 ASP461 ASP463 ASP515

  21. EC4-EC5 ineraction eith Ca+2611 GLU343 GLU397 ASP432 VAL433 ASP435

  22. EC1 EC2

  23. EC3 EC4

  24. EC5

  25. Cis-dimer protein-protein interaction Convex surface: Bottom of domain 2(lower parts of the B, D, and E strands) Concave surface: EC1 domain (strands C, D, and F)

  26. Cis-dimer protein-protein interaction(5A)

  27. Glycosylated amino acids

  28. EC2 glycosylation sites ASP154 PRO155 GLU186 THR188

  29. EC3 glycosylation sites LYS224 THR227 THR245 ASN270 THR273 LEU312 THR314 THR318 THR320 ALA335

  30. EC4 glycosylation sites ASN403 TYR406 THR407 VAL419 THR421 THR423 THR425

  31. EC5 glycosylation sites VAL524 ASN526

  32. Thanks for your attention!

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