3d65: Difference between revisions

Revision as of 09:58, 14 November 2018

Crystal structure of Textilinin-1, a Kunitz-type serine protease inhibitor from the Australian Common Brown snake venom, in complex with trypsin

Structural highlights

3d65 is a 2 chain structure with sequence from Bovin and Eastern brown snake. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	CA
Related:	3byb
Activity:	Trypsin, with EC number 3.4.21.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VKT1_PSETT] Strongly inhibits plasmin (Ki=0.44 nM) and trypsin (Ki=0.42 nM). Has little effect on plasma (Ki=1870 nM) and tissue (Ki=12900 nM) kallikreins. In vivo, reduces bleeding in a small animal model.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Masci PP, Whitaker AN, Sparrow LG, de Jersey J, Winzor DJ, Watters DJ, Lavin MF, Gaffney PJ. Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model. Blood Coagul Fibrinolysis. 2000 Jun;11(4):385-93. PMID:10847427
↑ Filippovich I, Sorokina N, Masci PP, de Jersey J, Whitaker AN, Winzor DJ, Gaffney PJ, Lavin MF. A family of textilinin genes, two of which encode proteins with antihaemorrhagic properties. Br J Haematol. 2002 Nov;119(2):376-84. PMID:12406072
↑ Flight S, Johnson L, Trabi M, Gaffney P, Lavin M, de Jersey J, Masci P. Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents. Pathophysiol Haemost Thromb. 2005;34(4-5):188-93. PMID:16707925 doi:https://dx.doi.org/10.1159/000092421
↑ Flight SM, Johnson LA, Du QS, Warner RL, Trabi M, Gaffney PJ, Lavin MF, de Jersey J, Masci PP. Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss. Br J Haematol. 2009 Apr;145(2):207-11. doi: 10.1111/j.1365-2141.2009.07605.x., Epub 2009 Feb 22. PMID:19236611 doi:https://dx.doi.org/10.1111/j.1365-2141.2009.07605.x
↑ Earl ST, Richards R, Johnson LA, Flight S, Anderson S, Liao A, de Jersey J, Masci PP, Lavin MF. Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms. Biochimie. 2012 Feb;94(2):365-73. doi: 10.1016/j.biochi.2011.08.003. Epub 2011, Aug 11. PMID:21843588 doi:https://dx.doi.org/10.1016/j.biochi.2011.08.003
↑ Millers EK, Johnson LA, Birrell GW, Masci PP, Lavin MF, de Jersey J, Guddat LW. The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake. PLoS One. 2013;8(1):e54104. doi: 10.1371/journal.pone.0054104. Epub 2013 Jan 15. PMID:23335990 doi:10.1371/journal.pone.0054104

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Masci PP, Whitaker AN, Sparrow LG, de Jersey J, Winzor DJ, Watters DJ, Lavin MF, Gaffney PJ. Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model. Blood Coagul Fibrinolysis. 2000 Jun;11(4):385-93. PMID:10847427

[2] Filippovich I, Sorokina N, Masci PP, de Jersey J, Whitaker AN, Winzor DJ, Gaffney PJ, Lavin MF. A family of textilinin genes, two of which encode proteins with antihaemorrhagic properties. Br J Haematol. 2002 Nov;119(2):376-84. PMID:12406072

[3] Flight S, Johnson L, Trabi M, Gaffney P, Lavin M, de Jersey J, Masci P. Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents. Pathophysiol Haemost Thromb. 2005;34(4-5):188-93. PMID:16707925 doi:https://dx.doi.org/10.1159/000092421

[4] Flight SM, Johnson LA, Du QS, Warner RL, Trabi M, Gaffney PJ, Lavin MF, de Jersey J, Masci PP. Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss. Br J Haematol. 2009 Apr;145(2):207-11. doi: 10.1111/j.1365-2141.2009.07605.x., Epub 2009 Feb 22. PMID:19236611 doi:https://dx.doi.org/10.1111/j.1365-2141.2009.07605.x

[5] Earl ST, Richards R, Johnson LA, Flight S, Anderson S, Liao A, de Jersey J, Masci PP, Lavin MF. Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms. Biochimie. 2012 Feb;94(2):365-73. doi: 10.1016/j.biochi.2011.08.003. Epub 2011, Aug 11. PMID:21843588 doi:https://dx.doi.org/10.1016/j.biochi.2011.08.003

[6] Millers EK, Johnson LA, Birrell GW, Masci PP, Lavin MF, de Jersey J, Guddat LW. The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake. PLoS One. 2013;8(1):e54104. doi: 10.1371/journal.pone.0054104. Epub 2013 Jan 15. PMID:23335990 doi:10.1371/journal.pone.0054104

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 15: / Line 15: @@
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d6/3d65_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d6/3d65_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 37: / Line 37: @@
 [[Category: Millers, E K.I]]
 [[Category: Blood]]
+[[Category: Calcium]]
 [[Category: Coagulation]]
 [[Category: Digestion]]

3d65: Difference between revisions

Revision as of 09:58, 14 November 2018

Crystal structure of Textilinin-1, a Kunitz-type serine protease inhibitor from the Australian Common Brown snake venom, in complex with trypsin

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools