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1mr8

From Proteopedia

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{{STRUCTURE_1mr8| PDB=1mr8 | SCENE= }}
{{STRUCTURE_1mr8| PDB=1mr8 | SCENE= }}
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'''MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN'''
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===MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10771424}}
==About this Structure==
==About this Structure==
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[[Category: Migration inhibitory factor_ related protein 8]]
[[Category: Migration inhibitory factor_ related protein 8]]
[[Category: S100 protein]]
[[Category: S100 protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:37:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:11:42 2008''

Revision as of 10:11, 27 July 2008

Image:1mr8.png

Template:STRUCTURE 1mr8

MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN

Template:ABSTRACT PUBMED 10771424

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

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