8api: Difference between revisions

Revision as of 12:59, 11 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:8api.png

Template:STRUCTURE 8api

THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISMTHE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM

Template:ABSTRACT PUBMED 2785270

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 Fri Jul 11 12:59:42 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:8api.gif|left|200px]]
+{{Seed}}
+[[Image:8api.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_8api|  PDB=8api  |  SCENE=  }}
-'''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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_2785270}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 2785270 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_2785270}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Tokuoka, R.]]
 [[Category: Proteinase inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:48:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 12:59:42 2008''