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The overall architecture of the fibrinogen molecule and aspects of its packing to form fibrin have been derived from a study of electron microscope images of ordered arrays.
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www.nature.com/nature/journal/v289/n5795/abs/289263a0.h...
www.nature.com/nature/journal/v289/n5795/abs/289263a0.html
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This subgroup includes the ligand-binding domain of the collagen-binding S.aureus MSCRAMM CNA, and many other structures previously classified as jelly rolls. Structure predictions suggest that the four fibrinogen-binding S.aureus MSCRAMMs identified so far would also contain the same DEv-IgG fold.
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www.nature.com/doifinder/10.1093/emboj/cdf619
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Fibrinogen is a complex multifunctional protein, which contains constitutive association sites (gammaXL, D:D, Da, Db) as well as cryptic sites that become exposed as a result of fibrinogen proteolysis by thrombin (EA, EB). ... ReviewThe structure and biological features of fibrinogen and fibrin.
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www.ncbi.nlm.nih.gov/pubmed/9579639
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The structure obtained for the fibrinogen gamma-chain segment is not affected by crystal packing and can provide the missing links to the recently reported ...
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www.ncbi.nlm.nih.gov/pmc/articles/PMC2144222/
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Cote, H. C.F., Lord, S. T., Pratt, K. P. (1998). gamma -Chain Dysfibrinogenemias: Molecular Structure-Function Relationships of Naturally Occurring Mutations in the gamma Chain of Human Fibrinogen. Blood 92: 2195-2212 [Full Text]
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jcb.rupress.org/cgi/content/abstract/5/1/11
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265, 838-843]. To examine the structural basis for this result, we have determined the crystal structure of bovine thrombin complexed with a synthetic peptide containing residues 1-23 of fibrinogen Aalpha and the F8Y mutation.
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www.medscape.com/medline/abstract/9307032
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The Medscape Journal ... Allergy & Clinical Immunology ... 9001-32-5 (Fibrinogen)
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www.medscape.com/medline/abstract/4281939
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T. S6derqvist and B. Blomb~ck: Fibrinogen Structure and Evolution .... The structure and function of fibrinogen and its interaction with thrombin are ...
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www.springerlink.com/index/V37230273106G3V5.pdf
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The researchers measured this change by pulling engineered strands of fibrinogen molecules using an atomic force microscope. This alpha-helical coiled-coil "spring" is a common motif in protein structure, first identified more than 50 years ago and so its stretchiness may have broader implications in biology and medicine.
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www.news-medical.net/news/2007/01/14/21403.aspx
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