1psi: Difference between revisions
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|PDB= 1psi |SIZE=350|CAPTION= <scene name='initialview01'>1psi</scene>, resolution 2.92Å | |PDB= 1psi |SIZE=350|CAPTION= <scene name='initialview01'>1psi</scene>, resolution 2.92Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SCC:THIOETHYL GROUP'>SCC</scene> | |LIGAND= <scene name='pdbligand=SCC:THIOETHYL+GROUP'>SCC</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ALPHA-1-ANTITRYPSIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ALPHA-1-ANTITRYPSIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1psi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1psi OCA], [http://www.ebi.ac.uk/pdbsum/1psi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1psi RCSB]</span> | |||
}} | }} | ||
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==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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Elliott, P R.]] | [[Category: Elliott, P R.]] | ||
[[Category: Lomas, D A.]] | [[Category: Lomas, D A.]] | ||
[[Category: acute phase]] | [[Category: acute phase]] | ||
[[Category: disease mutation]] | [[Category: disease mutation]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:04:00 2008'' | ||
