1fvu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1fvu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvu, resolution 1.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Line 1: Line 1:
-
[[Image:1fvu.gif|left|200px]]<br /><applet load="1fvu" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1fvu.gif|left|200px]]<br /><applet load="1fvu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fvu, resolution 1.80&Aring;" />
caption="1fvu, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF BOTROCETIN'''<br />
'''CRYSTAL STRUCTURE OF BOTROCETIN'''<br />
==Overview==
==Overview==
-
The binding of von Willebrand factor (vWF) to the platelet receptor, glycoprotein (GP) Ib-IX-V complex, has a key role in the initiation of, thrombus formation and is regulated by interactions with extracellular, matrix components under the influence of hemodynamic forces. To a certain, extent, these effects can be mimicked in vitro by two nonphysiologic, modulators, ristocetin and botrocetin. The latter, isolated from the venom, of the snake Bothrops jararaca, is a 31-kDa heterodimeric protein that, forms a soluble complex with vWF. As an initial step toward understanding, the mechanisms that regulate vWF function, we have solved the crystal, structure of botrocetin at 1.8 A resolution. Botrocetin exhibits homology, with other snake proteins, but contains only one metal binding site as, compared to two in Factor IX binding protein and Factor IX/X binding, protein and none in flavocetin. A distinctive feature of botrocetin is the, presence of a negatively charged surface that may play a role in the, association with the vWF A1 domain.
+
The binding of von Willebrand factor (vWF) to the platelet receptor, glycoprotein (GP) Ib-IX-V complex, has a key role in the initiation of thrombus formation and is regulated by interactions with extracellular matrix components under the influence of hemodynamic forces. To a certain extent, these effects can be mimicked in vitro by two nonphysiologic modulators, ristocetin and botrocetin. The latter, isolated from the venom of the snake Bothrops jararaca, is a 31-kDa heterodimeric protein that forms a soluble complex with vWF. As an initial step toward understanding the mechanisms that regulate vWF function, we have solved the crystal structure of botrocetin at 1.8 A resolution. Botrocetin exhibits homology with other snake proteins, but contains only one metal binding site as compared to two in Factor IX binding protein and Factor IX/X binding protein and none in flavocetin. A distinctive feature of botrocetin is the presence of a negatively charged surface that may play a role in the association with the vWF A1 domain.
==About this Structure==
==About this Structure==
-
1FVU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bothrops_jararaca Bothrops jararaca] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FVU OCA].
+
1FVU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bothrops_jararaca Bothrops jararaca] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVU OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Celikel, R.]]
[[Category: Celikel, R.]]
-
[[Category: McClintoc, R.A.]]
+
[[Category: McClintoc, R A.]]
-
[[Category: Ruggeri, Z.M.]]
+
[[Category: Ruggeri, Z M.]]
[[Category: Sen, U.]]
[[Category: Sen, U.]]
[[Category: Subbarao, G.]]
[[Category: Subbarao, G.]]
-
[[Category: Varughese, K.I.]]
+
[[Category: Varughese, K I.]]
[[Category: Vasudevan, S.]]
[[Category: Vasudevan, S.]]
[[Category: MG]]
[[Category: MG]]
Line 26: Line 26:
[[Category: von willbrand factor modulator]]
[[Category: von willbrand factor modulator]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:20:54 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:13 2008''

Revision as of 10:43, 21 February 2008


1fvu, resolution 1.80Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF BOTROCETIN

Overview

The binding of von Willebrand factor (vWF) to the platelet receptor, glycoprotein (GP) Ib-IX-V complex, has a key role in the initiation of thrombus formation and is regulated by interactions with extracellular matrix components under the influence of hemodynamic forces. To a certain extent, these effects can be mimicked in vitro by two nonphysiologic modulators, ristocetin and botrocetin. The latter, isolated from the venom of the snake Bothrops jararaca, is a 31-kDa heterodimeric protein that forms a soluble complex with vWF. As an initial step toward understanding the mechanisms that regulate vWF function, we have solved the crystal structure of botrocetin at 1.8 A resolution. Botrocetin exhibits homology with other snake proteins, but contains only one metal binding site as compared to two in Factor IX binding protein and Factor IX/X binding protein and none in flavocetin. A distinctive feature of botrocetin is the presence of a negatively charged surface that may play a role in the association with the vWF A1 domain.

About this Structure

1FVU is a Protein complex structure of sequences from Bothrops jararaca with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the von Willebrand factor modulator botrocetin., Sen U, Vasudevan S, Subbarao G, McClintock RA, Celikel R, Ruggeri ZM, Varughese KI, Biochemistry. 2001 Jan 16;40(2):345-52. PMID:11148028

Page seeded by OCA on Thu Feb 21 12:43:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools