1ZMF

C domain of human cyclophilin-33(hcyp33)

Summary for 1ZMF

• Entry DOI: 10.2210/pdb1zmf/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase E (2 entities in total)
• Functional Keywords: human cyclophilin-33, ppiase, isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9UNP9
• Total number of polymer chains: 1
• Total formula weight: 18230.75

Authors

Wang, T.,Yun, C.-H.,Gu, S.-Y.,Chang, W.-R.,Liang, D.-C. (deposition date: 2005-05-10, release date: 2005-08-02, Last modification date: 2024-03-13)

Primary citation

Wang, T.,Yun, C.-H.,Gu, S.-Y.,Chang, W.-R.,Liang, D.-C.
1.88A crystal structure of the C domain of hCyP33: A novel domain of peptidyl-prolyl cis-trans isomerase
Biochem.Biophys.Res.Commun., 333:845-849, 2005

PubMed Abstract: Cyclophilins (CyPs) are a widespreading protein family in living organisms and possess the activity of peptidyl-prolyl cis-trans isomerase (PPIase), which is inhibited by cyclosporin A (CsA). The human nuclear cyclophilin (hCyP33) is the first protein which was found to contain two RNA binding domains at the amino-terminus and a PPIase domain at the carboxyl-terminus. We isolated the hCyP33 gene from the human hematopoietic stem/progenitor cells and expressed it in Escherichia coli, and determined the crystal structure of the C domain of hCyP33 at 1.88 A resolution. The core structure is a beta-barrel covered by two alpha-helices. Superposition of the structure of the C domain of hCyP33 with the structure of CypA suggests that the C domain contains PPIase active site which binds to CsA. Furthermore, C domain seems to be able to bind with the Gag-encoded capsid (CA) of HIV-1 and may affect the viral replication of HIV-1. A key residue of the active site is changed from Ala-103-CypA to Ser-239-hCyP33, which may affect the PPIase domain/substrates interactions.

PubMed: 15963461
DOI: 10.1016/j.bbrc.2005.06.006

Experimental method

X-RAY DIFFRACTION (1.88 Å)