1ff7: Difference between revisions
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'''THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, 20 STRUCTURES''' | {{Structure | ||
|PDB= 1ff7 |SIZE=350|CAPTION= <scene name='initialview01'>1ff7</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, 20 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FF7 is a [ | 1FF7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FF7 OCA]. | ||
==Reference== | ==Reference== | ||
The effect of O-fucosylation on the first EGF-like domain from human blood coagulation factor VII., Kao YH, Lee GF, Wang Y, Starovasnik MA, Kelley RF, Spellman MW, Lerner L, Biochemistry. 1999 Jun 1;38(22):7097-110. PMID:[http:// | The effect of O-fucosylation on the first EGF-like domain from human blood coagulation factor VII., Kao YH, Lee GF, Wang Y, Starovasnik MA, Kelley RF, Spellman MW, Lerner L, Biochemistry. 1999 Jun 1;38(22):7097-110. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10353820 10353820] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: o- linked fucose]] | [[Category: o- linked fucose]] | ||
''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 11:08:18 2008'' | ||
Revision as of 12:08, 20 March 2008
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THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, 20 STRUCTURES
OverviewOverview
The first epidermal growth factor-like domain (EGF-1) from blood coagulation factor VII (FVII) contains two unusual O-linked glycosylation sites at Ser-52 and Ser-60. We report here a detailed study of the effect of O-fucosylation at Ser-60 on the structure of FVII EGF-1, its Ca2+-binding affinity, and its interaction with tissue factor (TF). The in vitro fucosylation of the nonglycosylated FVII EGF-1 was achieved by using O-fucosyltransferase purified from Chinese hamster ovary cells. Distance and dihedral constraints derived from NMR data were used to determine the solution structures of both nonglycosylated and fucosylated FVII EGF-1 in the presence of CaCl2. The overall structure of fucosylated FVII EGF-1 is very similar to the nonfucosylated form even for the residues near the fucosylation site. The Ca2+ dissociation constants (Kd) for the nonfucosylated and fucosylated FVII EGF-1 were found to be 16.4 +/- 1.8 and 8.6 +/- 1.4 mM, respectively. The FVII EGF-1 domain binds to the extracellular part of TF with a low affinity (Kd approximately 0. 6 mM), and the addition of fucose appears to have no effect on this affinity. These results indicate that the FVII EGF-1 alone cannot form a tight complex with TF and suggest that the high binding affinity of FVIIa for TF requires cooperative interaction among the four domains in FVII with TF. Although the fucose has no significant effect on the interaction between TF and the individual FVII EGF-1 domain, it may affect the interaction of full-length FVIIa with TF by influencing its Ca2+-binding affinity.
DiseaseDisease
Known diseases associated with this structure: Factor VII deficiency OMIM:[227500], Myocardial infarction, decreased susceptibility to OMIM:[227500]
About this StructureAbout this Structure
1FF7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The effect of O-fucosylation on the first EGF-like domain from human blood coagulation factor VII., Kao YH, Lee GF, Wang Y, Starovasnik MA, Kelley RF, Spellman MW, Lerner L, Biochemistry. 1999 Jun 1;38(22):7097-110. PMID:10353820
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