1jrr: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /> <applet load="1jrr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jrr, resolution 1.60Å" /> '''HUMAN PLASMINOGEN A...
 
OCA (talk | contribs)
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1jrr.gif|left|200px]]<br />
<applet load="1jrr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jrr, resolution 1.60&Aring;" />
'''HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2.[LOOP (66-98) DELETIONMUTANT] COMPLEXED WITH PEPTIDE MIMIckING THE REACTIVE CENTER LOOP'''<br />


==Overview==
==HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2.[LOOP (66-98) DELETIONMUTANT] COMPLEXED WITH PEPTIDE MIMIckING THE REACTIVE CENTER LOOP==
The structure of the serpin, plasminogen activator inhibitor type-2, (PAI-2), in a complex with a peptide mimicking its reactive center loop, (RCL) has been determined at 1.6-A resolution. The structure shows the, relaxed state serpin structure with a prominent six-stranded beta-sheet., Clear electron density is seen for all residues in the peptide. The P1, residue of the peptide binds to a well defined pocket at the base of PAI-2, that may be important in determining the specificity of protease, inhibition. The stressed-to-relaxed state (S --&gt; R) transition in PAI-2, can be modeled as the relative motion between a quasirigid core domain and, a smaller segment comprising helix hF and beta-strands s1A, s2A, and s3A., A comparison of the Ramachandran plots of the stressed and relaxed state, PAI-2 structures reveals the location of several hinge regions connecting, these two domains. The hinge regions cluster in three locations on the, structure, ensuring a cooperative S --&gt; R transition. We hypothesize that, the hinge formed by the conserved Gly(206) on beta-strand s3A in the, breach region of PAI-2 effects the S --&gt; R transition by altering its, backbone torsion angles. This torsional change is due to the binding of, the P14 threonine of the RCL to the open breach region of PAI-2.
<StructureSection load='1jrr' size='340' side='right'caption='[[1jrr]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jrr]] is a 2 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=1JRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JRR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></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=1jrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jrr OCA], [https://pdbe.org/1jrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jrr RCSB], [https://www.ebi.ac.uk/pdbsum/1jrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jrr ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jr/1jrr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jrr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the serpin, plasminogen activator inhibitor type-2 (PAI-2), in a complex with a peptide mimicking its reactive center loop (RCL) has been determined at 1.6-A resolution. The structure shows the relaxed state serpin structure with a prominent six-stranded beta-sheet. Clear electron density is seen for all residues in the peptide. The P1 residue of the peptide binds to a well defined pocket at the base of PAI-2 that may be important in determining the specificity of protease inhibition. The stressed-to-relaxed state (S --&gt; R) transition in PAI-2 can be modeled as the relative motion between a quasirigid core domain and a smaller segment comprising helix hF and beta-strands s1A, s2A, and s3A. A comparison of the Ramachandran plots of the stressed and relaxed state PAI-2 structures reveals the location of several hinge regions connecting these two domains. The hinge regions cluster in three locations on the structure, ensuring a cooperative S --&gt; R transition. We hypothesize that the hinge formed by the conserved Gly(206) on beta-strand s3A in the breach region of PAI-2 effects the S --&gt; R transition by altering its backbone torsion angles. This torsional change is due to the binding of the P14 threonine of the RCL to the open breach region of PAI-2.


==About this Structure==
Crystal structure of the complex of plasminogen activator inhibitor 2 with a peptide mimicking the reactive center loop.,Jankova L, Harrop SJ, Saunders DN, Andrews JL, Bertram KC, Gould AR, Baker MS, Curmi PM J Biol Chem. 2001 Nov 16;276(46):43374-82. Epub 2001 Aug 23. PMID:11546761<ref>PMID:11546761</ref>
1JRR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACE and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JRR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of the complex of plasminogen activator inhibitor 2 with a peptide mimicking the reactive center loop., Jankova L, Harrop SJ, Saunders DN, Andrews JL, Bertram KC, Gould AR, Baker MS, Curmi PM, J Biol Chem. 2001 Nov 16;276(46):43374-82. Epub 2001 Aug 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11546761 11546761]
</div>
<div class="pdbe-citations 1jrr" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Plasminogen activator inhibitor|Plasminogen activator inhibitor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Andrews, J.L.]]
[[Category: Andrews JL]]
[[Category: Baker, M.S.]]
[[Category: Baker MS]]
[[Category: Bertram, K.C.]]
[[Category: Bertram KC]]
[[Category: Curmi, P.M.G.]]
[[Category: Curmi PMG]]
[[Category: Gould, A.R.]]
[[Category: Gould AR]]
[[Category: Harrop, S.J.]]
[[Category: Harrop SJ]]
[[Category: Jankova, L.]]
[[Category: Jankova L]]
[[Category: Saunders, D.N.]]
[[Category: Saunders DN]]
[[Category: ACE]]
[[Category: BME]]
[[Category: peptide binding]]
[[Category: serpin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:43:48 2007''

Latest revision as of 22:04, 26 March 2025

HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2.[LOOP (66-98) DELETIONMUTANT] COMPLEXED WITH PEPTIDE MIMIckING THE REACTIVE CENTER LOOP

1jrr, resolution 1.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA