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| | <StructureSection load='1by7' size='340' side='right'caption='[[1by7]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1by7' size='340' side='right'caption='[[1by7]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1by7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BY7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1by7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BY7 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1by7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by7 OCA], [http://pdbe.org/1by7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1by7 RCSB], [http://www.ebi.ac.uk/pdbsum/1by7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1by7 ProSAT]</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]] 2Å</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=1by7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by7 OCA], [https://pdbe.org/1by7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1by7 RCSB], [https://www.ebi.ac.uk/pdbsum/1by7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1by7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAI2_HUMAN PAI2_HUMAN]] Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1. | + | [https://www.uniprot.org/uniprot/PAI2_HUMAN PAI2_HUMAN] Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Curmi, P M.G]] | + | [[Category: Curmi PMG]] |
| - | [[Category: Harrop, S J]] | + | [[Category: Harrop SJ]] |
| - | [[Category: King, G C]] | + | [[Category: King GC]] |
| - | [[Category: Mabbutt, B C]] | + | [[Category: Mabbutt BC]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Serpin]]
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| Structural highlights
Function
PAI2_HUMAN Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1.
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
BACKGROUND: Plasminogen activator inhibitor 2 (PAI-2) is a member of the serpin family of protease inhibitors that function via a dramatic structural change from a native, stressed state to a relaxed form. This transition is mediated by a segment of the serpin termed the reactive centre loop (RCL); the RCL is cleaved on interaction with the protease and becomes inserted into betasheet A of the serpin. Major questions remain as to what factors facilitate this transition and how they relate to protease inhibition. RESULTS: The crystal structure of a mutant form of human PAI-2 in the stressed state has been determined at 2.0 A resolution. The RCL is completely disordered in the structure. An examination of polar residues that are highly conserved across all serpins identifies functionally important regions. A buried polar cluster beneath betasheet A (the so-called 'shutter' region) is found to stabilise both the stressed and relaxed forms via a rearrangement of hydrogen bonds. CONCLUSIONS: A statistical analysis of interstrand interactions indicated that the shutter region can be used to discriminate between inhibitory and non-inhibitory serpins. This analysis implied that insertion of the RCL into betasheet A up to residue P8 is important for protease inhibition and hence the structure of the complex formed between the serpin and the target protease.
The crystal structure of plasminogen activator inhibitor 2 at 2.0 A resolution: implications for serpin function.,Harrop SJ, Jankova L, Coles M, Jardine D, Whittaker JS, Gould AR, Meister A, King GC, Mabbutt BC, Curmi PM Structure. 1999 Jan 15;7(1):43-54. PMID:10368272[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Harrop SJ, Jankova L, Coles M, Jardine D, Whittaker JS, Gould AR, Meister A, King GC, Mabbutt BC, Curmi PM. The crystal structure of plasminogen activator inhibitor 2 at 2.0 A resolution: implications for serpin function. Structure. 1999 Jan 15;7(1):43-54. PMID:10368272
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