8api: Difference between revisions
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'''THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM''' | '''THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM''' | ||
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==About this Structure== | ==About this Structure== | ||
8API is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry | 8API is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6api 6api]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8API OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Loebermann, H.]] | [[Category: Loebermann, H.]] | ||
[[Category: Tokuoka, R.]] | [[Category: Tokuoka, R.]] | ||
[[Category: | [[Category: Proteinase inhibitor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:48:37 2008'' | |||
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Revision as of 22:48, 4 May 2008
THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM
OverviewOverview
The S variant of the human alpha 1-antitrypsin with E-264----V, is responsible for a mild alpha 1-antitrypsin deficiency quite common in the European population. S protein specifically cleaved at the susceptible peptide bond was crystallized and its crystal structure determined and refined to 3.1 A resolution. The S variant crystallizes isomorphous to the normal M variant. The difference Fourier electron density map shows the E----V change as outstanding residual density. In addition, small structural changes of the main polypeptide chain radiate from the site of mutation and affect parts far removed from it. By the mutation, internal hydrogen bonds and salt linkages of E-264 to Y-38 and K-487, respectively, are lost. They cause the far-reaching slight distortions and are probably related to the reduced thermal stability of the S mutant. They may also be responsible for slower folding of the polypeptide chain and the clinical symptoms of alpha 1-antitrypsin deficiency. In a theoretical study by molecular dynamics methods simulations of the M and S proteins were made and the results analysed with respect to structural and dynamic properties and compared with the experimental results. There is a significant correlation between experimental and theoretical results in some respects.
About this StructureAbout this Structure
8API is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 6api. Full crystallographic information is available from OCA.
ReferenceReference
The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism., Engh R, Lobermann H, Schneider M, Wiegand G, Huber R, Laurell CB, Protein Eng. 1989 Mar;2(6):407-15. PMID:2785270 Page seeded by OCA on Sun May 4 22:48:37 2008