1BOY
EXTRACELLULAR REGION OF HUMAN TISSUE FACTOR
Summary for 1BOY
Entry DOI | 10.2210/pdb1boy/pdb |
Descriptor | HUMAN TISSUE FACTOR (2 entities in total) |
Functional Keywords | initiator of blood coagulation in vertebrates, cofactor for factor viia, class 2 cytokine receptor, glycoprotein, blood coagulation |
Biological source | Homo sapiens (human) |
Cellular location | Membrane; Single-pass type I membrane protein: P13726 |
Total number of polymer chains | 1 |
Total formula weight | 24826.51 |
Authors | Boys, C.W.G.,Tuddenham, E.G.D.,Harlos, K. (deposition date: 1996-01-11, release date: 1996-06-10, Last modification date: 2024-10-30) |
Primary citation | Harlos, K.,Martin, D.M.,O'Brien, D.P.,Jones, E.Y.,Stuart, D.I.,Polikarpov, I.,Miller, A.,Tuddenham, E.G.,Boys, C.W. Crystal structure of the extracellular region of human tissue factor. Nature, 370:662-666, 1994 Cited by PubMed Abstract: Tissue factor is a cell-surface glycoprotein receptor which initiates the blood coagulation cascade after vessel injury by interacting with blood clotting factor VII/VIIa and which is implicated in various pathological processes. When bound to tissue factor, factor VII is readily converted to the active protease factor VIIa by trace amounts of factors Xa, IXa or VIIa. Human tissue factor consists of 263 residues, the first 219 of which comprise the extracellular region. We have determined the crystal structure of the extracellular region at a resolution of 2.2 A. Tissue factor consists of two immunoglobulin-like domains associated through an extensive, novel, interdomain interface region. The binding site for factor VII lies at the interface region and involves residues from domain 1 and an extended loop (binding 'finger') of domain 2. This is the first reported structure of a representative of the class 2 cytokine receptor family, which also includes interferon-alpha, interferon-gamma (refs 2, 3) and interleukin-10 (ref. 4) receptors. PubMed: 8065454DOI: 10.1038/370662a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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