1a33: Difference between revisions

Revision as of 15:53, 30 June 2008

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File:1a33.png

Template:STRUCTURE 1a33

PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYIPEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI

Template:ABSTRACT PUBMED 9655334

About this StructureAbout this Structure

1A33 is a Single protein structure of sequence from Brugia malayi. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi., Mikol V, Ma D, Carlow CK, Protein Sci. 1998 Jun;7(6):1310-6. PMID:9655334

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-'''PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI'''
+===PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI===
-==Overview==
+<!--
-Cyclophilins are a family of proteins that exhibit peptidyl-prolyl cis-trans isomerase activity and bind the immunosuppressive agent cyclosporin A (CsA). Brugia malayi is a filarial nematode parasite of humans, for which a cyclophilin-like domain was identified at the N-terminal of a protein containing 843 amino acid residues. There are two differences in sequence in the highly conserved CsA binding site: A histidine and a lysine replace a tryptophan and an alanine, respectively. The crystal structure of this domain has been determined by the molecular replacement method and refined to an R-factor of 16.9% at 2.15 A resolution. The overall structure is similar to other cyclophilins; however, major differences occur in two loops. Comparison of the CsA binding site of this domain with members of the cyclophilin family shows significant structural differences, which can account for the reduced sensitivity of the Brugia malayi protein to inhibition by CsA.
+The line below this paragraph, {{ABSTRACT_PUBMED_9655334}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9655334}}
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 [[Category: Peptidyl-prolyl cis-tran]]
 [[Category: Peptidylprolyl isomerase]]
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