1a33: Difference between revisions

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[[Image:1a33.~~gif~~|left|200px]]

[[Image:1a33.png|left|200px]]

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~~'''~~PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI~~'''~~

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

~~==Overview==~~

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~~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

(as it appears on PubMed at http://www.pubmed.gov), where 9655334 is the PubMed ID number.

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==About this Structure==

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[[Category: Peptidyl-prolyl cis-tran]]

[[Category: Peptidylprolyl isomerase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 09~~:44:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:53:51 2008''

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-[[Image:1a33.gif|left|200px]]
+{{Seed}}
+[[Image:1a33.png|left|200px]]
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 {{STRUCTURE_1a33|  PDB=1a33  |  SCENE=  }}
-'''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
+(as it appears on PubMed at http://www.pubmed.gov), where 9655334 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9655334}}
 ==About this Structure==
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 [[Category: Peptidyl-prolyl cis-tran]]
 [[Category: Peptidylprolyl isomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:44:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:53:51 2008''