Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding.
about
Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism.The influence of hinge region residue Glu-381 on antithrombin allostery and metastabilityA Simple Method for Discovering Druggable, Specific Glycosaminoglycan-Protein Systems. Elucidation of Key Principles from Heparin/Heparan Sulfate-Binding ProteinsFinding a needle in a haystack: development of a combinatorial virtual screening approach for identifying high specificity heparin/heparan sulfate sequence(s).Fondaparinux: a potential new therapy for HIT.A peptide found by phage display discriminates a specific structure of a trisaccharide in heparin.Antithrombin regulates matriptase activity involved in plasmin generation, syndecan shedding, and HGF activation in keratinocytes.Mechanisms of glycosaminoglycan activation of the serpins in hemostasis.Heparin-binding domains in vascular biology.Mutation of the H-helix in antithrombin decreases heparin stimulation of protease inhibition.The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Elucidating the specificity of non-heparin-based conformational activators of antithrombin for factor Xa inhibition.Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.Estimating glycosaminoglycan-protein interaction affinity: water dominates the specific antithrombin-heparin interaction.Effects of glycosylation on heparin binding and antithrombin activation by heparin.The heparin-binding site of antithrombin is crucial for antiangiogenic activityAntiangiogenic forms of antithrombin specifically bind to the anticoagulant heparin sequence.Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities.Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation.Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin.Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.Antithrombin conformational modulation by D-myo-inositol 3,4,5,6-tetrakisphosphate (TMI), a novel scaffold for the development of antithrombotic agents.An analysis approach to identify specific functional sites in orthologous proteins using sequence and structural information: application to neuroserpin reveals regions that differentially regulate inhibitory activity.Dynamic properties of the native free antithrombin from molecular dynamics simulations: computational evidence for solvent- exposed Arg393 side chain.
P2860
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P2860
Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Lysine 114 of antithrombin is ...... parin pentasaccharide binding.
@en
type
label
Lysine 114 of antithrombin is ...... parin pentasaccharide binding.
@en
prefLabel
Lysine 114 of antithrombin is ...... parin pentasaccharide binding.
@en
P2093
P2860
P356
P1476
Lysine 114 of antithrombin is ...... parin pentasaccharide binding.
@en
P2093
P2860
P304
43809-43817
P356
10.1074/JBC.M105294200
P407
P577
2001-09-20T00:00:00Z