1. Volume 31, Issue 4, Pages 598-606 (August 2008)
Structure of Activated Thrombin-Activatable Fibrinolysis Inhibitor, a Molecular Link between Coagulation and Fibrinolysis 
Laura Sanglas, Zuzana Valnickova, Joan L. Arolas, Irantzu Pallarés, Tibisay Guevara, Maria Solà, Torsten Kristensen, Jan J. Enghild, Francesc X. Aviles, F. Xavier Gomis-Rüth 
Molecular Cell 
Volume 31, Issue 4, Pages (August 2008)
DOI: /j.molcel
Copyright © 2008 Elsevier Inc. Terms and Conditions

2. Figure 1 Alignment of B-Type MCPs
Sequence alignment of bovine, human, rat, and mouse TAFI, human PCPB1, and porcine PCPB. The corresponding UniProt sequence database access codes and the percentage of sequence identity with human TAFI within overlapping residues are shown preceding the second and third blocks of sequences, respectively. Signal peptides are shown over yellow background. The TAFI activation cleavage site is indicated by red scissors. The traditional sequential numbering and the structure-based numbering of TAFI employed throughout the text are shown above and below each alignment block, respectively. The latter numbering was established for porcine PCPB to fit that of archetypal bovine CPA1 (Coll et al., 1991). This entails that the prodomain is numbered separately (1A–95A) from the active enzyme moiety (4–308) and that there is a one-residue insertion after position 188 in B-type MCPs, here named TAFI starts with Phe7A and has three extra unique one-residue insertions after positions 56, 150, and 235 of the mature enzyme moiety with respect to porcine PCPB, which are numbered 567, 1501, and 2356, respectively. In addition, TAFI displays three extra residues at the end of the prodomain, so that cleavage occurs at bond Arg98A-Ala4. Regular secondary structure elements for bovine TAFIa (helices as green cringles, α1–α7; β strands as red arrows, β1–β8; T1 and T2 for 1,4-turns of type I and II) are depicted above each sequence block. Identical residues in bovine and human TAFI are shown over blue background, and those identical in all four sequences are shown over magenta background. Positions reported to produce human TAFI or TAFIa variants with longer half-lives (Ceresa et al., 2006, 2007; Knecht et al., 2006; Schneider et al., 2002) are shown in green. Segments disordered in TAFIa are shown in red.
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2008 Elsevier Inc. Terms and Conditions

3. Figure 2 Structure of TAFIa in Its Complex with TCI
(A) Richardson plot of the complex showing TAFIa in standard orientation with yellow β strands (β1–β8), green α helices (α1–α7) and the catalytic zinc ion as a red sphere. Segment α5-Lα5β7-β7 is shown in orange, and the TAFI exosite is shown in magenta. The region of the proposed fibrinolysis switch is shown over gray background. TCI is shown for its NTD (light blue), linker (red) and CTD (navy blue). The disulfide bonds of TCI are also shown. The N and C termini of both molecules are labeled.
(B) Close-up view of (A) after a vertical rotation of ∼90° showing the proposed fibrinolysis switch region of TAFIa (yellow) superimposed with the equivalent region of human CPB1 (green). TAFIa regular secondary structure elements are labeled.
(C) Close-up view of (A) showing the TAFIa active site and the residues participating in the interaction with TCI CTD.
(D) Close-up view of (A) centered on the interaction area of TAFIa with TCI NTD and the participating residues.
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2008 Elsevier Inc. Terms and Conditions