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Blood, Vol. 108, Issue 6, 1887-1894, September 15, 2006 This Article Abstract Full Text Services Email this article to a friend Alert me to new issues of the journal Rights and Permissions Citing Articles Citing Articles via CrossRef Analysis of fibrinogen variants at 387Ile shows that the side chain of 387 and the tertiary structure of the C-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed - dimer formation Blood Kani et al. 108: 1887 Supplemental materials for: Kani et al Files in this Data Supplement: The putative structures of the fibrinogen γ-chain C-terminal residue of γ387 variants (JPG, 115 KB) - The wireframe views show residues that are within 6 Å of residue 387. The views of 387 variants were generated with Swiss-Pdb Viewer (http://www.expasy.ch/spdbv) from the protein databank file 3fib/pdb. A: 387I, B: 387R, C: 387L, D: 387M, E: 387A, F: 387D. Green and purple dotted lines show putative strong H-bonds and steric hindrance, respectively. This Article Abstract Full Text Services Email this article to a friend Alert me to new issues of the journal Rights and Permissions Citing Articles Citing Articles via CrossRef

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