1mr8

From Proteopedia

---

Revision as of 16:07, 12 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1mr8, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The structure of human MRP8 in the calcium-bound form was determined at, 1.9 A resolution by X-ray crystallography. The structure was initially, solved by MAD phasing of an ytterbium-substituted crystal and was refined, against data obtained from a Ca(2+)-bound crystal. The dimeric form of, MRP8 was stabilized by hydrophobic interactions between mutually wrapped, helices. There were two EF-hand motifs per monomer and each EF-hand bound, one Ca(2+) with a different affinity [the affinity of the C-terminal, EF-hand (EF-2) for Ca(2+) was stronger than that of the N-terminal EF-hand, (EF-1)]. Furthermore, replacement with Yb(3+) occurred in the C-terminal, EF-hand only, suggesting a more flexible nature for EF-2 than for EF-1., This, combined with previous observations that the helix in EF-2 (helix, III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for, Ca(2+)-induced conformational change.

Disease

Known disease associated with this structure: Earwax, wet/dry OMIM:[607040]

About this Structure

1MR8 is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.

Reference

The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution., Ishikawa K, Nakagawa A, Tanaka I, Suzuki M, Nishihira J, Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):559-66. PMID:10771424

Page seeded by OCA on Mon Nov 12 18:14:18 2007