Factor XI

1XX9, 1XXD, 1XXF, 1ZHM, 1ZHP, 1ZHR, 1ZJD, 1ZLR, 1ZMJ, 1ZML, 1ZMN, 1ZOM, 1ZPB, 1ZPC, 1ZPZ, 1ZRK, 1ZSJ, 1ZSK, 1ZSL, 1ZTJ, 1ZTK, 1ZTL, 2F83, 2FDA, 2J8J, 2J8L, 3BG8, 3SOR, 3SOS, 4CR5, 4CR9, 4CRA, 4CRB, 4CRC, 4CRD, 4CRE, 4CRF, 4CRG, 4NA7, 4NA8, 4TY6, 4TY7, 4WXI, 4X6M, 4X6N, 4X6O, 4X6P, 4Y8X, 4Y8Y, 4Y8Z, 4D7F, 5E2O, 5E2P, 4D76, 4D7G, 5EXL, 5I25, 5EXM, 5EOD, 5EXN, 5EOK2160109821ENSG00000088926ENSMUSG00000031645P03951Q91Y47NM_000128NM_019559NM_001354804NM_028066NP_000119NP_001341733NP_082342Factor XI or plasma thromboplastin antecedent is the zymogen form of factor XIa, one of the enzymes of the coagulation cascade. Like many other coagulation factors, it is a serine protease. In humans, Factor XI is encoded by the F11 gene.1xx9: Crystal Structure of the FXIa Catalytic Domain in Complex with EcotinM84R1xxd: Crystal Structure of the FXIa Catalytic Domain in Complex with mutated Ecotin1xxf: Crystal Structure of the FXIa Catalytic Domain in Complex with Ecotin Mutant (EcotinP)1zhm: Crystal Structure of the Catalytic Domain of the Coagulation Factor XIa in Complex with Benzamidine (S434A-T475A-K437 Mutant)1zhp: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with Benzamidine (S434A-T475A-K505 Mutant)1zhr: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with Benzamidine (S434A-T475A-C482S-K437A Mutant)1zjd: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with Kunitz Protease Inhibitor Domain of Protease Nexin II1zlr: Factor XI catalytic domain complexed with 2-guanidino-1-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)ethyl nicotinate1zmj: Crystal Structure of the Catalytic Domain of Factor XI in complex with 4-(guanidinomethyl)-phenylboronic acid1zml: Crystal Structure of the Catalytic Domain of Factor XI in complex with (R)-1-(4-(4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl)phenethyl)guanidine1zmn: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with (R)-1-(4-(4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl)phenyl)guanidine1zom: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in complex with a peptidomimetic Inhibitor1zpb: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with 4-Methyl-pentanoic acid {1--2-methyl-propyl}-amide1zpc: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with 2--N--3-methyl-butyramide1zpz: Factor XI catalytic domain complexed with N-((R)-1-(4-bromophenyl)ethyl)urea-Asn-Val-Arg-alpha-ketothiazole1zrk: Factor XI complexed with 3-hydroxypropyl 3-(7-amidinonaphthalene-1-carboxamido)benzenesulfonate1zsj: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in complex with N-(7-Carbamimidoyl-naphthalen-1-yl)-3-hydroxy-2-methyl-benzamide1zsk: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with 6-Carbamimidoyl-4-(3-hydroxy-2-methyl-benzoylamino)-naphthalene-2-carboxylic acid methyl ester1zsl: Factor XI complexed with a pyrimidinone inhibitor1ztj: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with 2-(5-Benzylamino-2-methylsulfanyl-6-oxo-6H-pyrimidin-1-yl)-N--acetamide1ztk: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with 2-(5-Amino-6-oxo-2-m-tolyl-6H-pyrimidin-1-yl)-N--acetamide1ztl: Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with N--2-{6-oxo-5--2-m-tolyl-6H-pyrimidin-1-yl}-acetamide2f83: Crystal structure at 2.9 Angstroms resolution of human plasma coagulation factor XI zymogen2fda: Crystal Structure of the Catalytic Domain of Human Coagulation Factor XIa in Complex with alpha-Ketothiazole Arginine Derived Ligand Factor XI or plasma thromboplastin antecedent is the zymogen form of factor XIa, one of the enzymes of the coagulation cascade. Like many other coagulation factors, it is a serine protease. In humans, Factor XI is encoded by the F11 gene. Factor XI (FXI) is produced by the liver and circulates as a homo-dimer in its inactive form. The plasma half-life of FXI is approximately 52 hours. The zymogen factor is activated into factor XIa by factor XIIa (FXIIa), thrombin, and FXIa itself; due to its activation by FXIIa, FXI is a member of the 'contact pathway' (which includes HMWK, prekallikrein, factor XII, factor XI, and factor IX). Factor XIa activates factor IX by selectively cleaving arg-ala and arg-val peptide bonds. Factor IXa, in turn, forms a complex with Factor VIIIa (FIXa-FVIIIa) and activates factor X. Inhibitors of factor XIa include protein Z-dependent protease inhibitor (ZPI, a member of the serine protease inhibitor/serpin class of proteins), which is independent of protein Z (its action on factor X, however, is protein Z-dependent, hence its name). Although synthesized as a single polypeptide chain, FXI circulates as a homodimer. Every chain has a relative molecular mass of approximately 80000. Typical plasma concentrations of FXI are 5 μg/mL, corresponding to a plasma concentration (of FXI dimers) of approximately 30 nM.The FXI gene is 23kb in length, has 15 exons, and is found on chromosome 4q32-35. Factor XI consists of four apple domains, that create a disk-like platform around the base of a fifth, catalytic serine protease domain.One contains a binding site for thrombin, another for high molecular weight kininogen, a third one for factor IX, heparin and glycoprotein Ib and the fourth is implicated in forming the factor XI homodimer, including a cysteine residue that creates a disulfide bond.