1qz2
From Proteopedia
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Crystal Structure of FKBP52 C-terminal Domain complex with the C-terminal peptide MEEVD of Hsp90
Overview
FK506-binding protein 52 (FKBP52), which binds FK506 and possesses, peptidylprolyl isomerase activity, is an important immunophilin involved, in the heterocomplex of steroid receptors with heat-shock protein 90. Here, we report the crystal structures of two overlapped fragments [N(1-260) and, C(145-459)] of FKBP52 and the complex with a C-terminal pentapeptide from, heat-shock protein 90. Based on the structures of these two overlapped, fragments, the complete putative structure of FKBP52 can be defined. The, structure of FKBP52 is composed of two consecutive FKBP domains, a, tetratricopeptide repeat domain and a short helical domain beyond the, final tetratricopeptide repeat motif. Key structural differences between, FKBP52 and FKBP51, including the relative orientations of the four domains, and some important residue substitutions, could account for the, differential functions of FKBPs.
About this Structure
1QZ2 is a Protein complex structure of sequences from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex., Wu B, Li P, Liu Y, Lou Z, Ding Y, Shu C, Ye S, Bartlam M, Shen B, Rao Z, Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8348-53. Epub 2004 May 24. PMID:15159550
Page seeded by OCA on Mon Nov 12 18:57:44 2007
Categories: Homo sapiens | Peptidylprolyl isomerase | Protein complex | Ding, Y. | Li, P. | Liu, Y. | Lou, Z. | Rao, Z. | Shen, B. | Shu, C. | Wu, B. | Chaperone | Heat shock | Isomerase | Rotamase
