Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding (Q27619526)

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A Lang

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A Karcher

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K Sichler

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E Kopetzki

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R Huber

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W Bode

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R A Engh

The coagulation cascade: initiation, maintenance, and regulation

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publication date

15 August 1999

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published in

Structure

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volume

7

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issue

8

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page(s)

989-96

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A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S

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Factor Xa-factor Va complex assembles in two dimensions with unexpectedly high affinity: an experimental and theoretical approach

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28 Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates

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Dramatic enhancement of the catalytic activity of coagulation factor IXa by alcohols

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X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B

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Structure of human des(1-45) factor Xa at 2.2 A resolution

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X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition

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Converting blood coagulation factor IXa into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants

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Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin

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Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its [...]

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The 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator

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Blood coagulation factor IX residues Glu78 and Arg94 provide a link between both epidermal growth factor-like domains that is crucial in the interaction with factor VIII light chain

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