1a33: Difference between revisions
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[[Image:1a33.gif|left|200px]] | [[Image:1a33.gif|left|200px]] | ||
'''PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI''' | {{Structure | ||
|PDB= 1a33 |SIZE=350|CAPTION= <scene name='initialview01'>1a33</scene>, resolution 2.15Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= BMCYP-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6279 Brugia malayi]) | |||
}} | |||
'''PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A33 is a [ | 1A33 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brugia_malayi Brugia malayi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A33 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9655334 9655334] | ||
[[Category: Brugia malayi]] | [[Category: Brugia malayi]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[Category: Mikol, V.]] | [[Category: Mikol, V.]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: peptidyl-prolyl cis- | [[Category: peptidyl-prolyl cis-tran]] | ||
[[Category: peptidylprolyl isomerase]] | [[Category: peptidylprolyl isomerase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:08 2008'' | ||
Revision as of 10:52, 20 March 2008
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| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | BMCYP-1 (Brugia malayi) | ||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI
OverviewOverview
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 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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