1psi: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /> <applet load="1psi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psi, resolution 2.92Å" /> '''INTACT RECOMBINED A...
 
No edit summary
Line 1: Line 1:
[[Image:1psi.gif|left|200px]]<br />
[[Image:1psi.gif|left|200px]]<br /><applet load="1psi" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1psi" size="450" color="white" frame="true" align="right" spinBox="true"  
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==
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.
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==
Line 11: Line 10:


==About this Structure==
==About this Structure==
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].  
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==
Line 18: Line 17:
[[Category: Serpins]]
[[Category: Serpins]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Abrahams, J.P.]]
[[Category: Abrahams, J P.]]
[[Category: Carrell, R.W.]]
[[Category: Carrell, R W.]]
[[Category: Elliott, P.R.]]
[[Category: Elliott, P R.]]
[[Category: Lomas, D.A.]]
[[Category: Lomas, D A.]]
[[Category: SCC]]
[[Category: SCC]]
[[Category: acute phase]]
[[Category: acute phase]]
Line 32: Line 31:
[[Category: signal]]
[[Category: signal]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:46:44 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:07 2008''

Revision as of 15:32, 21 February 2008

File:1psi.gif


1psi, resolution 2.92Å

Drag the structure with the mouse to rotate

INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU

OverviewOverview

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.

DiseaseDisease

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 StructureAbout 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.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 14:32:07 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA