PDBsum entry 1a33

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Isomerase PDB id
Protein chain
174 a.a.
Waters ×234

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Key reference
Title Crystal structure of the cyclophilin-Like domain from the parasitic nematode brugia malayi.
Authors V.Mikol, D.Ma, C.K.Carlow.
Ref. Protein Sci, 1998, 7, 1310-1316. [DOI no: 10.1002/pro.5560070606]
PubMed id 9655334
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a perfect match.
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.
Figure 1.
Fig. 1. Schematic representation f CypBm- I. All representing molecules were prepared with the program MOLSCRIPT Kraulis. 1991 ).
Figure 3.
Fig. 3. Stereopicture of the overlay of CypBm-1 on CypHA(a) and onCypHB(b).The C" trace of CypBm-l (continuous lines) is superimposed on that of CypHA(broken lines) (A) andon that o CypHB lines) B). Some residues of CypBm-1 are labeled.
The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1998, 7, 1310-1316) copyright 1998.
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