Figure 1.
Ligand binding sites within the 4 apple domains and catalytic domain of FXI. This figure distinguishes the domains of FXI according to color: A1 (orange), A2 (pink), A3 (blue), A4 (green), and catalytic (purple). The A1 domain mediates binding with thrombin (Ala45-Arg54, Val59-Arg70, Glu66, Lys83, and Gln84) and HK (Phe56-Ser86 and Val69-Arg83). The A2 domain mediates binding with HK (Asn106, Tyr107, Asn108, His127, Thr132, Ala134, His143, Ile146, Leu148, and His151) and FXIIa (residues unknown). The A3 domain mediates binding with thrombin (Asp204), FV (residues unknown), FIX (Ile183-Val191, Ser195-Ile197, and Phe260-Ser265), FXIIa (residues unknown), GPIbα (Ser248, Arg250, Lys255, Phe260, and Gln263), polyphosphate (Arg250, Ile251, Lys252, Lys253, Ser254, and Lys255), HK (Ala193-Ala205 and Leu239-Phe260), and SkM (residues unknown). The A4 domain mediates binding with thrombin (Asp280, Lys301) and FXIIa (Ala317-Gly350). The serine protease domain mediates binding with thrombin (Pro520), polyP (Lys529, Arg530, Arg532, Lys534, and Lys538), and natural inhibitors such as antithrombin, C1-inhibitor, nexin-1, nexin-2, and α-1 antitrypsin (Arg504, Lys505, Arg507, and Lys509). Residues that mediate binding are summarized in Table 1. Current and future studies using techniques, such as cryogenic electron microscopy, will hold promise in validating epitopes for these binding partners. PolyP, polyphosphate; SkM, skeletal muscle myosin.

Ligand binding sites within the 4 apple domains and catalytic domain of FXI. This figure distinguishes the domains of FXI according to color: A1 (orange), A2 (pink), A3 (blue), A4 (green), and catalytic (purple). The A1 domain mediates binding with thrombin (Ala45-Arg54, Val59-Arg70, Glu66, Lys83, and Gln84) and HK (Phe56-Ser86 and Val69-Arg83). The A2 domain mediates binding with HK (Asn106, Tyr107, Asn108, His127, Thr132, Ala134, His143, Ile146, Leu148, and His151) and FXIIa (residues unknown). The A3 domain mediates binding with thrombin (Asp204), FV (residues unknown), FIX (Ile183-Val191, Ser195-Ile197, and Phe260-Ser265), FXIIa (residues unknown), GPIbα (Ser248, Arg250, Lys255, Phe260, and Gln263), polyphosphate (Arg250, Ile251, Lys252, Lys253, Ser254, and Lys255), HK (Ala193-Ala205 and Leu239-Phe260), and SkM (residues unknown). The A4 domain mediates binding with thrombin (Asp280, Lys301) and FXIIa (Ala317-Gly350). The serine protease domain mediates binding with thrombin (Pro520), polyP (Lys529, Arg530, Arg532, Lys534, and Lys538), and natural inhibitors such as antithrombin, C1-inhibitor, nexin-1, nexin-2, and α-1 antitrypsin (Arg504, Lys505, Arg507, and Lys509). Residues that mediate binding are summarized in Table 1. Current and future studies using techniques, such as cryogenic electron microscopy, will hold promise in validating epitopes for these binding partners. PolyP, polyphosphate; SkM, skeletal muscle myosin.

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