1by7

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[[Image:1by7.gif|left|200px]]<br /><applet load="1by7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1by7.gif|left|200px]]
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caption="1by7, resolution 2.0&Aring;" />
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'''HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2. LOOP (66-98) DELETION MUTANT'''<br />
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{{Structure
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|PDB= 1by7 |SIZE=350|CAPTION= <scene name='initialview01'>1by7</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2. LOOP (66-98) DELETION MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BY7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://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].
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1BY7 is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368272 10368272]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10368272 10368272]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:24 2008''

Revision as of 08:17, 20 March 2008


PDB ID 1by7

Drag the structure with the mouse to rotate
, resolution 2.0Å
Coordinates: save as pdb, mmCIF, xml



HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2. LOOP (66-98) DELETION MUTANT


Overview

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.

About this Structure

1BY7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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