1deq

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(New page: 200px<br /><applet load="1deq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1deq, resolution 3.5&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1deq.gif|left|200px]]<br /><applet load="1deq" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1deq, resolution 3.5&Aring;" />
'''THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)'''<br />
'''THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)'''<br />
==Overview==
==Overview==
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Here we report the crystal structure at approximately 4-A resolution of a, selectively proteolyzed bovine fibrinogen. This key component in, hemostasis is an elongated 340-kDa glycoprotein in the plasma that upon, activation by thrombin self-assembles to form the fibrin clot. The, crystals are unusual because they are made up of end-to-end bonded, molecules that form flexible filaments. We have visualized the entire, coiled-coil region of the molecule, which has a planar sigmoidal shape., The primary polymerization receptor pockets at the ends of the molecule, face the same way throughout the end-to-end bonded filaments, and based on, this conformation, we have developed an improved model of the two-stranded, protofibril that is the basic building block in fibrin. Near the middle of, the coiled-coil region, the plasmin-sensitive segment is a hinge about, which the molecule adopts different conformations. This segment also, includes the boundary between the three- and four-stranded portions of the, coiled coil, indicating the location on the backbone that anchors the, extended flexible Aalpha arm. We suggest that a flexible branch point in, the molecule may help accommodate variability in the structure of the, fibrin clot.
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Here we report the crystal structure at approximately 4-A resolution of a selectively proteolyzed bovine fibrinogen. This key component in hemostasis is an elongated 340-kDa glycoprotein in the plasma that upon activation by thrombin self-assembles to form the fibrin clot. The crystals are unusual because they are made up of end-to-end bonded molecules that form flexible filaments. We have visualized the entire coiled-coil region of the molecule, which has a planar sigmoidal shape. The primary polymerization receptor pockets at the ends of the molecule face the same way throughout the end-to-end bonded filaments, and based on this conformation, we have developed an improved model of the two-stranded protofibril that is the basic building block in fibrin. Near the middle of the coiled-coil region, the plasmin-sensitive segment is a hinge about which the molecule adopts different conformations. This segment also includes the boundary between the three- and four-stranded portions of the coiled coil, indicating the location on the backbone that anchors the extended flexible Aalpha arm. We suggest that a flexible branch point in the molecule may help accommodate variability in the structure of the fibrin clot.
==About this Structure==
==About this Structure==
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1DEQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEQ OCA].
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1DEQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEQ OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Brown, J.H.]]
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[[Category: Brown, J H.]]
[[Category: Cohen, C.]]
[[Category: Cohen, C.]]
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[[Category: Henschen-Edman, A.H.]]
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[[Category: Henschen-Edman, A H.]]
[[Category: Jun, G.]]
[[Category: Jun, G.]]
[[Category: Volkmann, N.]]
[[Category: Volkmann, N.]]
[[Category: coiled-coil]]
[[Category: coiled-coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:13:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:54 2008''

Revision as of 10:15, 21 February 2008


1deq, resolution 3.5Å

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THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)

Overview

Here we report the crystal structure at approximately 4-A resolution of a selectively proteolyzed bovine fibrinogen. This key component in hemostasis is an elongated 340-kDa glycoprotein in the plasma that upon activation by thrombin self-assembles to form the fibrin clot. The crystals are unusual because they are made up of end-to-end bonded molecules that form flexible filaments. We have visualized the entire coiled-coil region of the molecule, which has a planar sigmoidal shape. The primary polymerization receptor pockets at the ends of the molecule face the same way throughout the end-to-end bonded filaments, and based on this conformation, we have developed an improved model of the two-stranded protofibril that is the basic building block in fibrin. Near the middle of the coiled-coil region, the plasmin-sensitive segment is a hinge about which the molecule adopts different conformations. This segment also includes the boundary between the three- and four-stranded portions of the coiled coil, indicating the location on the backbone that anchors the extended flexible Aalpha arm. We suggest that a flexible branch point in the molecule may help accommodate variability in the structure of the fibrin clot.

About this Structure

1DEQ is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

The crystal structure of modified bovine fibrinogen., Brown JH, Volkmann N, Jun G, Henschen-Edman AH, Cohen C, Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):85-90. PMID:10618375

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