1P53
The Crystal Structure of ICAM-1 D3-D5 fragment
Summary for 1P53
| Entry DOI | 10.2210/pdb1p53/pdb |
| Descriptor | Intercellular adhesion molecule-1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | igsf domain, beta-sheet, dimer, cell adhesion |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 58986.23 |
| Authors | Yang, Y.,Jun, C.D.,Liu, J.H.,Zhang, R.,Jochimiak, A.,Springer, T.A.,Wang, J.H. (deposition date: 2003-04-24, release date: 2004-05-04, Last modification date: 2024-10-09) |
| Primary citation | Yang, Y.,Jun, C.D.,Liu, J.H.,Zhang, R.,Joachimiak, A.,Springer, T.A.,Wang, J.H. Structural basis for dimerization of ICAM-1 on the cell surface. Mol.Cell, 14:269-276, 2004 Cited by PubMed Abstract: 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. PubMed: 15099525DOI: 10.1016/S1097-2765(04)00204-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.06 Å) |
Structure validation
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