1A33

PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI

Summary for 1A33

• Entry DOI: 10.2210/pdb1a33/pdb
• Descriptor: PEPTIDYLPROLYL ISOMERASE (2 entities in total)
• Functional Keywords: isomerase, peptidyl-prolyl cis-trans, peptidylprolyl isomerase
• Biological source: Brugia malayi
• Total number of polymer chains: 1
• Total formula weight: 19504.42

Authors

Mikol, V.,Ma, D.,Carlow, C.K.S. (deposition date: 1998-01-27, release date: 1998-07-29, Last modification date: 2024-05-22)

Primary citation

Mikol, V.,Ma, D.,Carlow, C.K.
Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi.
Protein Sci., 7:1310-1316, 1998

PubMed Abstract: 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.

PubMed: 9655334

Experimental method

X-RAY DIFFRACTION (2.15 Å)