A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
James JR, Oliveira MI, Carmo AM, Iaboni A, Davis SJ. (2006), Nat Methods. 3, 1001-6
TCR triggering without ligands
The animation shows the resting T-cell surface and the changes in organization of signaling proteins that occur when the cell interacts with a bilayer containing the cell adhesion molecule CD2, leading to ligand-independent TCR triggering.
The early stages of the animation strive to portray the rapid movements of the proteins and the crowded nature of the T-cell surface. The interaction of CD2 (in the bilayer) with a non-signaling form of CD48 (on the T cell) results in close-contact formation and the exclusion of CD45. Because contact with the bilayer is over a large area, the exclusion of CD45 results in strong TCR phosphorylation by non-excluded Lck kinase, leading to ZAP70 recruitment and calcium signaling in the absence of TCR ligands.
The animation finishes with an image of a bilayer-contacting Jurkat T-cell from the present study showing the distribution of CD45 (green) and Lck (red). The molecules shown are: the TCR (terracotta), CD45 (light green); Lck in an active conformation (red); CD48 (dark green) and CD2 (yellow). The structures were built using the Build Structure function in UCSF Chimera. The animation was built using Blender software.
Top Ten Papers
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Crystal structure of a soluble CD28-Fab complex
Evans EJ, Esnouf RM, Manso-Sancho R, Gilbert RJ, James JR, Yu C, Fennelly JA, Vowles C, Hanke T, Walse B, Hünig T, Sørensen P, Stuart DI, Davis SJ. (2005), Nat Immunol. 6, 271-9
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The T cell surface – how well do we know it?
Evans EJ, Hene L, Sparks LM, Dong T, Retiere C, Fennelly JA, Manso-Sancho R, Powell J, Braud VM, Rowland-Jones SL, McMichael AJ, Davis SJ. (2003), Immunity. 19, 213-23
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LICOS, a primordial costimulatory ligand?
Brodie D, Collins AV, Iaboni A, Fennelly JA, Sparks LM, Xu XN, van der Merwe PA, Davis SJ. (2000), Curr Biol. 10, 333-6
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Structure and dimerization of a soluble form of B7-1
Ikemizu S, Gilbert RJ, Fennelly JA, Collins AV, Harlos K, Jones EY, Stuart DI, Davis SJ. (2000), Immunity. 12, 51-60
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The role of charged residues mediating low affinity protein-protein recognition at the cell surface by CD2
Davis SJ, Davies EA, Tucknott MG, Jones EY, van der Merwe PA. (1998), Proc Natl Acad Sci U S A. 95, 5490-4
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The structure and ligand interactions of CD2: implications for T-cell function
Davis SJ, van der Merwe PA. (1996), Immunol Today. 17, 177-87
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Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2
Davis SJ, Puklavec MJ, Ashford DA, Harlos K, Jones EY, Stuart DI, Williams AF. (1993), Protein Eng. 6, 229-32
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Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2
Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI. (1992), Nature. 360, 232-9
