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1mr8

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[[Image:1mr8.gif|left|200px]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB]</span>
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'''MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN'''
'''MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN'''
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[[Category: Nishihira, J.]]
[[Category: Nishihira, J.]]
[[Category: Tanaka, I.]]
[[Category: Tanaka, I.]]
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[[Category: calcium-binding protein]]
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[[Category: Calcium-binding protein]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: mad]]
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[[Category: Mad]]
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[[Category: migration inhibitory factor_ related protein 8]]
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[[Category: Migration inhibitory factor_ related protein 8]]
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[[Category: s100 protein]]
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[[Category: S100 protein]]
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Revision as of 22:37, 2 May 2008

Template:STRUCTURE 1mr8

MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN


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.

About this Structure

1MR8 is a Single protein structure of sequence from Homo sapiens. 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 Sat May 3 01:37:36 2008

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