Journal of Molecular Biology
Designation of sequences involved in the “coiled-coil” interdomainal connections in fibrinogen: Construction of an atomic scale model☆
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2012, Food HydrocolloidsCitation Excerpt :Each one is composed of three non-identical polypeptide chains (Aα, Bβ and γ), held together by 29 disulfide bonds. Its conformation is organized in a central globular hydrophobic nodule (E domain) containing the N-terminals of all six chains and two peripheral globular hydrophobic nodules (D domains) (Brown, Litvinov, Discher, & Weisel, 2007; Colafranceschi, Giuliani, & Colosimo, 2008; Doolittle, Goldbaum, & Doolittle, 1978) that consist of the C-terminal ends except of that corresponding to Aα chains (αC regions), which interact intramolecularly with each other at the central E region through their hydrophobic regions (Litvinov et al., 2007; Medved, Gorkun, & Privalov, 1983; Tsurupa, Tsonev, & Medved, 2002; Weisel & Medved, 2001). However, under specific conditions, αC domains can dissociate and become available for intermolecular interactions.
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2011, Advances in Protein Chemistry and Structural BiologyCitation Excerpt :In 1959, Hall and Slayter identified by electron microscopy that fibrinogen has a trinodular structure comprised of three spherical particles bound together by a thread-like structure (Hall and Slayter, 1959). Subsequent structural studies confirmed the initial low resolution findings and demonstrated the fibrinogen molecule to be composed of two D regions separated from a central E region by two coiled-coil regions (Doolittle et al., 1978). After the publication of many crystal structures of the fibrinogen D region (Spraggon et al., 1997), E region (Madrazo et al., 2001), bovine fibrinogen (Brown et al., 2000), and chicken fibrinogen (Yang et al., 2001), in 2009 the crystal structure of the human fibrinogen molecule was published by Kollman et al. (2009) at approximately 3.3 Å resolution (Fig. 3).
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The Chemistry Department Computer Center is supported by National Institutes of Health grant no. RR-00757. Other aspects of this work were supported by National Institutes of Health grant no. HL-18576.