1jrr

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(New page: 200px<br /> <applet load="1jrr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jrr, resolution 1.60&Aring;" /> '''HUMAN PLASMINOGEN A...)
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[[Image:1jrr.gif|left|200px]]<br /><applet load="1jrr" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1jrr" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1jrr, resolution 1.60&Aring;" />
caption="1jrr, resolution 1.60&Aring;" />
'''HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2.[LOOP (66-98) DELETIONMUTANT] COMPLEXED WITH PEPTIDE MIMIckING THE REACTIVE CENTER LOOP'''<br />
'''HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2.[LOOP (66-98) DELETIONMUTANT] COMPLEXED WITH PEPTIDE MIMIckING THE REACTIVE CENTER LOOP'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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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].
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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 <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRR OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Andrews, J.L.]]
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[[Category: Andrews, J L.]]
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[[Category: Baker, M.S.]]
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[[Category: Baker, M S.]]
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[[Category: Bertram, K.C.]]
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[[Category: Bertram, K C.]]
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[[Category: Curmi, P.M.G.]]
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[[Category: Curmi, P M.G.]]
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[[Category: Gould, A.R.]]
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[[Category: Gould, A R.]]
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[[Category: Harrop, S.J.]]
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[[Category: Harrop, S J.]]
[[Category: Jankova, L.]]
[[Category: Jankova, L.]]
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[[Category: Saunders, D.N.]]
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[[Category: Saunders, D N.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: BME]]
[[Category: BME]]
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[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:43:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:59 2008''

Revision as of 11:26, 21 February 2008


1jrr, resolution 1.60Å

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

Overview

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 --> 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 --> 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 --> 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

1JRR is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

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

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