1mr8
From Proteopedia
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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.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding protein]] |
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Mad]] |
| - | [[Category: | + | [[Category: Migration inhibitory factor_ related protein 8]] |
| - | [[Category: | + | [[Category: S100 protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:37:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:37, 2 May 2008
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
