1toc

From Proteopedia

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Current revision

STRUCTURE OF SERINE PROTEINASE

Structural highlights

1toc is a 12 chain structure with sequence from Bos taurus and Ornithodoros moubata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THRB_BOVIN Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity).

Evolutionary Conservation

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

Publication Abstract from PubMed

Ornithodorin, isolated from the blood sucking soft tick Ornithodoros moubata, is a potent (Ki = 10(-12) M) and highly selective thrombin inhibitor. Internal sequence homology indicates a two domain protein. Each domain resembles the Kunitz inhibitor basic pancreatic trypsin inhibitor (BPTI) and also the tick anticoagulant peptide (TAP) isolated from the same organism. The 3.1 A crystal structure of the ornithodorin-thrombin complex confirms that both domains of ornithodorin exhibit a distorted BPTI-like fold. The N-terminal portion and the C-terminal helix of each domain are structurally very similar to BPTI, whereas the regions corresponding to the binding loop of BPTI adopt different conformations. Neither of the two 'reactive site loops' of ornithodorin contacts the protease in the ornithodorin-thrombin complex. Instead, the N-terminal residues of ornithodorin bind to the active site of thrombin, reminiscent of the thrombin-hirudin interaction. The C-terminal domain binds at the fibrinogen recognition exosite. Molecular recognition of its target protease by this double-headed Kunitz-type inhibitor diverges considerably from other members of this intensely studied superfamily. The complex structure provides a model to explain the perplexing results of mutagenesis studies on the TAP-factor Xa interaction.

The ornithodorin-thrombin crystal structure, a key to the TAP enigma?,van de Locht A, Stubbs MT, Bode W, Friedrich T, Bollschweiler C, Hoffken W, Huber R EMBO J. 1996 Nov 15;15(22):6011-7. PMID:8947023^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van de Locht A, Stubbs MT, Bode W, Friedrich T, Bollschweiler C, Hoffken W, Huber R. The ornithodorin-thrombin crystal structure, a key to the TAP enigma? EMBO J. 1996 Nov 15;15(22):6011-7. PMID:8947023

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1toc"

@@ Line 3: / Line 3: @@
 <StructureSection load='1toc' size='340' side='right'caption='[[1toc]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1toc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Argasid_tick Argasid tick] and [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TOC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1toc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Ornithodoros_moubata Ornithodoros moubata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TOC FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1toc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1toc OCA], [https://pdbe.org/1toc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1toc RCSB], [https://www.ebi.ac.uk/pdbsum/1toc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1toc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/THRB_BOVIN THRB_BOVIN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). [[https://www.uniprot.org/uniprot/ORNT_ORNMO ORNT_ORNMO]] Potent (Ki = 10(-12) M) and highly selective thrombin inhibitor.
+[https://www.uniprot.org/uniprot/THRB_BOVIN THRB_BOVIN] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/to/1toc_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 30: / Line 30: @@
 ==See Also==
+*[[Proteinase 3D structures|Proteinase 3D structures]]
 *[[Thrombin 3D Structures|Thrombin 3D Structures]]
 == References ==
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Argasid tick]]
+[[Category: Bos taurus]]
-[[Category: Bovin]]
 [[Category: Large Structures]]
-[[Category: Thrombin]]
+[[Category: Ornithodoros moubata]]
-[[Category: Bode, W]]
+[[Category: Bode W]]
-[[Category: Huber, R]]
+[[Category: Huber R]]
-[[Category: Locht, A Van De]]
+[[Category: Van De Locht A]]
-[[Category: Acute phase]]
-[[Category: Gamma-carboxyglutamic acid]]
-[[Category: Hydrolase]]
-[[Category: Kringle]]
-[[Category: Liver]]
-[[Category: Serine protease kunitz-like inhibitor]]
-[[Category: Vitamin k]]
-[[Category: Zymogen]]

1toc

From Proteopedia

Current revision

STRUCTURE OF SERINE PROTEINASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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