Structural basis for dimerization of ICAM-1 on the cell surface.
We have determined the 3.0 A crystal structure of the three C-terminal domains 3-5 (D3-D5) of ICAM-1. Combined with the previously known N-terminal two-domain structure (D1D2), a model of an entire ICAM-1 extracellular fragment has been constructed. This model should represent a general architecture of other ICAM family members, particularly ICAM-3 and ICAM-5. The observed intimate dimerization interaction at D4 and a stiff D4-D5 stem-like architecture provide a good structural explanation for the existence of preformed ICAM-1 cis dimers on the cell membrane. Together with another dimerization interface at D1, a band-like one-dimensional linear cluster of ICAM-1 on an antigen-presenting cell (APC) surface can be envisioned, which might explain the formation of an immunological synapse between an activated T cell and APC which is critical for T cell receptor signaling.
Yang
Yuting
Y
Dana-Farber Cancer Institute, Boston, MA 02115, USA.
Jun
Chang-Duk
CD
Liu
Jin-Huan
JH
Zhang
Rongguang
R
Joachimiak
Andrzej
A
Springer
Timothy A
TA
Wang
Jia-Huai
JH
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D016466:CHO Cells; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D017124:Conserved Sequence; D006224:Cricetinae; D003412:Cricetulus; D018360:Crystallography, X-Ray; D019281:Dimerization; D004220:Disulfides; D006031:Glycosylation; D057927:Hydrophobic and Hydrophilic Interactions; D016023:Integrins / Q000378:metabolism; D018799:Intercellular Adhesion Molecule-1 / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D004220:Disulfides; D016023:Integrins; D018799:Intercellular Adhesion Molecule-1