1a33

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[[Image:1a33.gif|left|200px]]
[[Image:1a33.gif|left|200px]]
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{{Structure
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|PDB= 1a33 |SIZE=350|CAPTION= <scene name='initialview01'>1a33</scene>, resolution 2.15&Aring;
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The line below this paragraph, containing "STRUCTURE_1a33", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= BMCYP-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6279 Brugia malayi])
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|DOMAIN=
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{{STRUCTURE_1a33| PDB=1a33 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a33 OCA], [http://www.ebi.ac.uk/pdbsum/1a33 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a33 RCSB]</span>
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'''PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI'''
'''PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI'''
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[[Category: Ma, D.]]
[[Category: Ma, D.]]
[[Category: Mikol, V.]]
[[Category: Mikol, V.]]
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[[Category: isomerase]]
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[[Category: Isomerase]]
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[[Category: peptidyl-prolyl cis-tran]]
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[[Category: Peptidyl-prolyl cis-tran]]
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[[Category: peptidylprolyl isomerase]]
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[[Category: Peptidylprolyl isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:44:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:32:16 2008''
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Revision as of 06:44, 2 May 2008

Template:STRUCTURE 1a33

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.

About this Structure

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

Reference

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 Page seeded by OCA on Fri May 2 09:44:09 2008

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