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1mr8
From Proteopedia
(New page: 200px<br /> <applet load="1mr8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mr8, resolution 1.9Å" /> '''MIGRATION INHIBITORY...) |
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| - | [[Image:1mr8.gif|left|200px]]<br /> | + | [[Image:1mr8.gif|left|200px]]<br /><applet load="1mr8" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mr8" size=" | + | |
caption="1mr8, resolution 1.9Å" /> | caption="1mr8, resolution 1.9Å" /> | ||
'''MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN'''<br /> | '''MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of human MRP8 in the calcium-bound form was determined at | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MR8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MR8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: s100 protein]] | [[Category: s100 protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:14 2008'' |
Revision as of 11:58, 21 February 2008
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MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN
Contents |
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 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
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