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1cyn

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1cyn, resolution 1.85Å ()
Non-Standard Residues: , , , , ,
Gene: CYCLOPHILIN (Homo sapiens)
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
Related: 1bck, 1c5f, 1csa, 1cwa, 1cwb, 1cwc, 1cwf, 1cwh, 1cwi, 1cwj, 1cwk, 1cwl, 1cwm, 1cwo, 1cya, 1cyb, 1ikf, 1m63, 1mf8, 1mik, 1qng, 1qnh, 1xq7, 2esl, 2oju, 2poy, 2rma, 2rmb, 2rmc, 2wfj, 2x2c, 2x7k, 2z6w, 3bo7, 3cys, 3eov
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN

Publication Abstract from PubMed

The crystal structure of a complex between recombinant human cyclophilin B (CypB) and a cyclosporin A (CsA) analog has been determined and refined at 1.85-A resolution to a crystallographic R factor of 16.0%. The overall structures of CypB and of cyclophilin A (CypA) are similar; however, significant differences occur in two loops and at the N and C termini. The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. The network of the water-mediated contacts is also essentially conserved. The higher potency of the CypB/CsA complex versus CypA/CsA in inhibiting the Ca(2+)- and calmodulin-dependent protein phosphatase calcineurin is discussed in terms of the structural differences between the two complexes. The three residues Arg90, Lys113, and Ala128 and the loop containing Arg158 on the surface of CypB are likely to modulate the differences in calcineurin inhibition between CypA and CypB.

X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain., Mikol V, Kallen J, Walkinshaw MD, Proc Natl Acad Sci U S A. 1994 May 24;91(11):5183-6. PMID:8197205

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Disease

[PPIB_HUMAN] Defects in PPIB are the cause of osteogenesis imperfecta type 9 (OI9) [MIM:259440]. OI9 is a connective tissue disorder characterized by bone fragility, low bone mass and bowing of limbs due to multiple fractures. Short limb dwarfism and blue sclerae are observed in some but not all patients.[1][2]

Function

[PPIB_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

About this Structure

1cyn is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Mikol V, Kallen J, Walkinshaw MD. X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain. Proc Natl Acad Sci U S A. 1994 May 24;91(11):5183-6. PMID:8197205
  • Mikol V, Kallen J, Pflugl G, Walkinshaw MD. X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J Mol Biol. 1993 Dec 20;234(4):1119-30. PMID:8263916 doi:http://dx.doi.org/10.1006/jmbi.1993.1664
  • Carpentier M, Allain F, Haendler B, Slomianny MC, Spik G. Delineation of the calcineurin-interacting region of cyclophilin B. Protein Sci. 2000 Dec;9(12):2386-93. PMID:11206060 doi:10.1110/ps.9.12.2386
  1. van Dijk FS, Nesbitt IM, Zwikstra EH, Nikkels PG, Piersma SR, Fratantoni SA, Jimenez CR, Huizer M, Morsman AC, Cobben JM, van Roij MH, Elting MW, Verbeke JI, Wijnaendts LC, Shaw NJ, Hogler W, McKeown C, Sistermans EA, Dalton A, Meijers-Heijboer H, Pals G. PPIB mutations cause severe osteogenesis imperfecta. Am J Hum Genet. 2009 Oct;85(4):521-7. doi: 10.1016/j.ajhg.2009.09.001. Epub 2009 , Sep 24. PMID:19781681 doi:10.1016/j.ajhg.2009.09.001
  2. Barnes AM, Carter EM, Cabral WA, Weis M, Chang W, Makareeva E, Leikin S, Rotimi CN, Eyre DR, Raggio CL, Marini JC. Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N Engl J Med. 2010 Feb 11;362(6):521-8. doi: 10.1056/NEJMoa0907705. Epub 2010 Jan, 20. PMID:20089953 doi:10.1056/NEJMoa0907705

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