1a21
From Proteopedia
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| - | [[Image:1a21.gif|left|200px]] | + | [[Image:1a21.gif|left|200px]] |
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| - | '''TISSUE FACTOR (TF) FROM RABBIT''' | + | {{Structure |
| + | |PDB= 1a21 |SIZE=350|CAPTION= <scene name='initialview01'>1a21</scene>, resolution 2.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''TISSUE FACTOR (TF) FROM RABBIT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A21 is a [ | + | 1A21 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A21 OCA]. |
==Reference== | ==Reference== | ||
| - | Hinge bending within the cytokine receptor superfamily revealed by the 2.4 A crystal structure of the extracellular domain of rabbit tissue factor., Muller YA, Kelley RF, de Vos AM, Protein Sci. 1998 May;7(5):1106-15. PMID:[http:// | + | Hinge bending within the cytokine receptor superfamily revealed by the 2.4 A crystal structure of the extracellular domain of rabbit tissue factor., Muller YA, Kelley RF, de Vos AM, Protein Sci. 1998 May;7(5):1106-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9605315 9605315] |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:43 2008'' |
Revision as of 07:51, 20 March 2008
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| , resolution 2.35Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
TISSUE FACTOR (TF) FROM RABBIT
Overview
Tissue factor (TF), a member of the cytokine receptor superfamily, is the obligate cofactor of coagulation factor VIIa (FVIIa), and has a pivotal role in initiating the extrinsic pathway of blood coagulation through formation of the TF x FVIIa complex. The crystal structure of the extracellular portion of rabbit TF has been solved at 2.35 A resolution and refined to a crystallographic R-value of 19.1% (free R-value, 27.7%). Like the human homologue, the extracellular portion consists of two fibronectin type III domains connected by a short alpha-helical segment. Unexpectedly, the two molecules in the crystallographic asymmetric unit differ in their relative domain-domain orientation, revealing unsuspected hinge motion consisting of a rotation of about 12.7 degrees around an axis intersecting the linker segment at residue 106. Superposition of rabbit tissue factor with free and bound human tissue factor allows for the detection of an identical, albeit smaller, hinge motion in human TF induced upon binding of FVIIa. This raises the possibility that a very similar hinge axis may be present in other members of the cytokine receptor superfamily.
About this Structure
1A21 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Hinge bending within the cytokine receptor superfamily revealed by the 2.4 A crystal structure of the extracellular domain of rabbit tissue factor., Muller YA, Kelley RF, de Vos AM, Protein Sci. 1998 May;7(5):1106-15. PMID:9605315
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