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[[Image:1atu.jpg|left|200px]]
{{Seed}}
[[Image:1atu.png|left|200px]]


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{{STRUCTURE_1atu|  PDB=1atu  |  SCENE=  }}  
{{STRUCTURE_1atu|  PDB=1atu  |  SCENE=  }}  


'''UNCLEAVED ALPHA-1-ANTITRYPSIN'''
===UNCLEAVED ALPHA-1-ANTITRYPSIN===




==Overview==
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BACKGROUND: The protein alpha1-antitrypsin is a prototype member of the serpin (serine protease inhibitor) family and is known to inhibit the activity of neutrophil elastase in the lower respiratory tract. Members of this family undergo a large structural rearrangement upon binding to a target protease, involving cleavage of the reactive-site loop. This loop is then inserted into the main body of the enzyme following the opening of a central beta sheet, leading to stabilization of the structure. Random mutageneses of alpha1-antitrypsin identified various mutations that stabilize the native structure and retard the insertion of the reactive-site loop. Structural studies of these mutations may reveal the mechanism of the conformational change. RESULTS: We have determined the three-dimensional structure of an uncleaved alpha1-antitrypsin with seven such stabilizing mutations (hepta alpha1-antitrypsin) at 2.7 A resolution. From the comparison of the structure with other serpin structures, we found that hepta alpha1-antitrypsin is stabilized due to the release of various strains that exist in native wild type alpha1-antitrypsin, including unfavorable hydrophobic interactions in the central hydrophobic core. The reactive-site loop of hepta alpha1-antitrypsin is an extended strand, different from that of the previously determined structure of another uncleaved alpha1-antitrypsin, and indicates the inherent flexibility of the loop. CONCLUSIONS: The present structural study suggests that the uncleaved alpha1-antitrypsin has many folding defects which can be improved by mutations. These folding defects seem to be utilized in a coordinated fashion in the regulation of the conformational switch of alpha1-antitrypsin. Some of the defects, represented by the Phe51 region and possibly the Met374 and the Thr59 regions, are part of the sheet-opening mechanism.
The line below this paragraph, {{ABSTRACT_PUBMED_8939743}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_8939743}}


==About this Structure==
==About this Structure==
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[[Category: Serine protease inhibitor]]
[[Category: Serine protease inhibitor]]
[[Category: Stabilizing mutation]]
[[Category: Stabilizing mutation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:41:03 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:34:57 2008''

Revision as of 14:34, 30 June 2008

File:1atu.png


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1atu, resolution 2.70Å (default scene)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



UNCLEAVED ALPHA-1-ANTITRYPSIN

Template:ABSTRACT PUBMED 8939743

About this Structure

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

Reference

The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A., Ryu SE, Choi HJ, Kwon KS, Lee KN, Yu MH, Structure. 1996 Oct 15;4(10):1181-92. PMID:8939743

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