2hft: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2hft |SIZE=350|CAPTION= <scene name='initialview01'>2hft</scene>, resolution 1.69Å | |PDB= 2hft |SIZE=350|CAPTION= <scene name='initialview01'>2hft</scene>, resolution 1.69Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hft OCA], [http://www.ebi.ac.uk/pdbsum/2hft PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hft RCSB]</span> | |||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==Overview== | ||
Exposure of blood to cells expressing tissue factor results in formation of a high-affinity complex with factor VIIa, initiating the extrinsic pathway of blood coagulation by the activation of factors IX and X. The structure of the extracellular portion of tissue factor was refined to a crystallographic R-value of 20.4% to a resolution of 1.69 A against synchroton data collected from a flash-frozen crystal. The structure consists of two fibronectin type III modules whose hydrophobic cores merge in the domain-domain interface, suggesting that the extracellular portion serves as a relatively rigid template for factor VIIa binding. Analysis of the hydrophobic core of each individual module identifies a cluster of residues forming a packing motif centered on Trp25 which appears to be characteristic for fibronectin type III modules. Comparison of the structure to that of the human growth hormone receptor, which belongs to a different class (class I) of the same cytokine receptor superfamily, shows that the structure of the individual domains is very similar but that the relative domain-domain orientation differs greatly. Even though the WSXWS box characteristic of the class I cytokine receptors is not present in tissue factor, the analogous residues have the identical polyproline helical conformation. Mapping of residues important for biological activity on the structure shows that all these are located on Beta-strands in a small number of distinct clusters, on the opposite side of the molecule compared to the ligand binding determinants of the growth hormone receptor. | Exposure of blood to cells expressing tissue factor results in formation of a high-affinity complex with factor VIIa, initiating the extrinsic pathway of blood coagulation by the activation of factors IX and X. The structure of the extracellular portion of tissue factor was refined to a crystallographic R-value of 20.4% to a resolution of 1.69 A against synchroton data collected from a flash-frozen crystal. The structure consists of two fibronectin type III modules whose hydrophobic cores merge in the domain-domain interface, suggesting that the extracellular portion serves as a relatively rigid template for factor VIIa binding. Analysis of the hydrophobic core of each individual module identifies a cluster of residues forming a packing motif centered on Trp25 which appears to be characteristic for fibronectin type III modules. Comparison of the structure to that of the human growth hormone receptor, which belongs to a different class (class I) of the same cytokine receptor superfamily, shows that the structure of the individual domains is very similar but that the relative domain-domain orientation differs greatly. Even though the WSXWS box characteristic of the class I cytokine receptors is not present in tissue factor, the analogous residues have the identical polyproline helical conformation. Mapping of residues important for biological activity on the structure shows that all these are located on Beta-strands in a small number of distinct clusters, on the opposite side of the molecule compared to the ligand binding determinants of the growth hormone receptor. | ||
==About this Structure== | ==About this Structure== | ||
| Line 28: | Line 28: | ||
[[Category: Muller, Y A.]] | [[Category: Muller, Y A.]] | ||
[[Category: Vos, A M.De.]] | [[Category: Vos, A M.De.]] | ||
[[Category: coagulation factor]] | [[Category: coagulation factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:29:47 2008'' | ||
Revision as of 03:29, 31 March 2008
| |||||||
| , resolution 1.69Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN TISSUE FACTOR AT 1.7 ANGSTROMS RESOLUTION
OverviewOverview
Exposure of blood to cells expressing tissue factor results in formation of a high-affinity complex with factor VIIa, initiating the extrinsic pathway of blood coagulation by the activation of factors IX and X. The structure of the extracellular portion of tissue factor was refined to a crystallographic R-value of 20.4% to a resolution of 1.69 A against synchroton data collected from a flash-frozen crystal. The structure consists of two fibronectin type III modules whose hydrophobic cores merge in the domain-domain interface, suggesting that the extracellular portion serves as a relatively rigid template for factor VIIa binding. Analysis of the hydrophobic core of each individual module identifies a cluster of residues forming a packing motif centered on Trp25 which appears to be characteristic for fibronectin type III modules. Comparison of the structure to that of the human growth hormone receptor, which belongs to a different class (class I) of the same cytokine receptor superfamily, shows that the structure of the individual domains is very similar but that the relative domain-domain orientation differs greatly. Even though the WSXWS box characteristic of the class I cytokine receptors is not present in tissue factor, the analogous residues have the identical polyproline helical conformation. Mapping of residues important for biological activity on the structure shows that all these are located on Beta-strands in a small number of distinct clusters, on the opposite side of the molecule compared to the ligand binding determinants of the growth hormone receptor.
About this StructureAbout this Structure
2HFT is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1HFT. The following page contains interesting information on the relation of 2HFT with [Tissue Factor]. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the extracellular domain of human tissue factor refined to 1.7 A resolution., Muller YA, Ultsch MH, de Vos AM, J Mol Biol. 1996 Feb 16;256(1):144-59. PMID:8609606
Page seeded by OCA on Mon Mar 31 03:29:47 2008