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1psi

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(New page: 200px<br /> <applet load="1psi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psi, resolution 2.92&Aring;" /> '''INTACT RECOMBINED A...)
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[[Image:1psi.gif|left|200px]]<br />
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[[Image:1psi.gif|left|200px]]<br /><applet load="1psi" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1psi" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1psi, resolution 2.92&Aring;" />
caption="1psi, resolution 2.92&Aring;" />
'''INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU'''<br />
'''INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU'''<br />
==Overview==
==Overview==
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The reactive site loop of the serpin family of serine proteinase, inhibitors is flexible and can adopt a number of diverse conformations. A, 2.9 A resolution structure of alpha 1-antitrypsin-the principal proteinase, inhibitor in human plasma-shows the loop in a stable canonical, conformation matching that found in all other families of serine, proteinase inhibitors. This unexpected finding in the absence of loop, insertion into the body of the molecule favours a two-stage mechanism of, inhibition and provides a model for the heparin activation of, antithrombin. The beta-pleated strand conformation of the loop also, accounts for the polymerization of the serpins in disease and for their, association with other beta-sheet structures, most notably the, beta-amyloid of Alzheimer's disease.
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The reactive site loop of the serpin family of serine proteinase inhibitors is flexible and can adopt a number of diverse conformations. A 2.9 A resolution structure of alpha 1-antitrypsin-the principal proteinase inhibitor in human plasma-shows the loop in a stable canonical conformation matching that found in all other families of serine proteinase inhibitors. This unexpected finding in the absence of loop insertion into the body of the molecule favours a two-stage mechanism of inhibition and provides a model for the heparin activation of antithrombin. The beta-pleated strand conformation of the loop also accounts for the polymerization of the serpins in disease and for their association with other beta-sheet structures, most notably the beta-amyloid of Alzheimer's disease.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1PSI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SCC as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1PSI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb53_1.html Serpins]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PSI OCA].
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1PSI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SCC:'>SCC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1PSI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb53_1.html Serpins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSI OCA].
==Reference==
==Reference==
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[[Category: Serpins]]
[[Category: Serpins]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Abrahams, J.P.]]
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[[Category: Abrahams, J P.]]
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[[Category: Carrell, R.W.]]
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[[Category: Carrell, R W.]]
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[[Category: Elliott, P.R.]]
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[[Category: Elliott, P R.]]
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[[Category: Lomas, D.A.]]
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[[Category: Lomas, D A.]]
[[Category: SCC]]
[[Category: SCC]]
[[Category: acute phase]]
[[Category: acute phase]]
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[[Category: signal]]
[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:46:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:07 2008''

Revision as of 12:32, 21 February 2008


1psi, resolution 2.92Å

Drag the structure with the mouse to rotate

INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU

Contents

Overview

The reactive site loop of the serpin family of serine proteinase inhibitors is flexible and can adopt a number of diverse conformations. A 2.9 A resolution structure of alpha 1-antitrypsin-the principal proteinase inhibitor in human plasma-shows the loop in a stable canonical conformation matching that found in all other families of serine proteinase inhibitors. This unexpected finding in the absence of loop insertion into the body of the molecule favours a two-stage mechanism of inhibition and provides a model for the heparin activation of antithrombin. The beta-pleated strand conformation of the loop also accounts for the polymerization of the serpins in disease and for their association with other beta-sheet structures, most notably the beta-amyloid of Alzheimer's disease.

Disease

Known diseases associated with this structure: Emphysema OMIM:[107400], Emphysema-cirrhosis OMIM:[107400], Hemorrhagic diathesis due to antithrombin Pittsburgh OMIM:[107400], Pulmonary disease, chronic obstructive, susceptibility to OMIM:[107400]

About this Structure

1PSI is a Single protein structure of sequence from Homo sapiens with as ligand. The following page contains interesting information on the relation of 1PSI with [Serpins]. Full crystallographic information is available from OCA.

Reference

Inhibitory conformation of the reactive loop of alpha 1-antitrypsin., Elliott PR, Lomas DA, Carrell RW, Abrahams JP, Nat Struct Biol. 1996 Aug;3(8):676-81. PMID:8756325

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