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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-2-10
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-13630928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-13993227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-1942070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-1948029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-2258925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-2673537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-2771651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-3090046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-3480524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-4071058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-460425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-500644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-527944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-601755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-6224704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-6383194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-7338923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-739546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-7453823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-8236112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-845954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-8514790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-8916221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-8918191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-8940292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-9016719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-9194178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-9207064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-9333233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10618375-9628725
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
97
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
85-90
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10618375-Animals,
pubmed-meshheading:10618375-Cattle,
pubmed-meshheading:10618375-Crystallization,
pubmed-meshheading:10618375-Crystallography, X-Ray,
pubmed-meshheading:10618375-Endopeptidases,
pubmed-meshheading:10618375-Fibrinogen,
pubmed-meshheading:10618375-Models, Molecular,
pubmed-meshheading:10618375-Molecular Sequence Data,
pubmed-meshheading:10618375-Protein Conformation
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pubmed:year |
2000
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pubmed:articleTitle |
The crystal structure of modified bovine fibrinogen.
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pubmed:affiliation |
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454-9110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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