2hft

From Proteopedia
Revision as of 23:25, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2hft" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hft, resolution 1.69Å" /> '''THE CRYSTAL STRUCTU...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:2hft.gif


2hft, resolution 1.69Å

Drag the structure with the mouse to rotate

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.

DiseaseDisease

Known disease associated with this structure: Esophageal squamous cell carcinoma OMIM:[606551]

About this StructureAbout this Structure

2HFT is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. This structure superseeds 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 Nov 12 22:31:59 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA