1mhc

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(New page: 200px<br /><applet load="1mhc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mhc, resolution 2.1&Aring;" /> '''MODEL OF MHC CLASS I ...)
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caption="1mhc, resolution 2.1&Aring;" />
'''MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION'''<br />
'''MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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H2-M3 is a class Ib MHC molecule of the mouse with a 10(4)-fold preference, for binding N-formylated peptides. To elucidate the basis of this unusual, specificity, we expressed and crystallized a soluble form of M3 with a, formylated nonamer peptide, fMYFINILTL, and determined the structure by, X-ray crystallography. M3, refined at 2.1 A resolution, resembles class la, MHC molecules in its overall structure, but differs in the peptide-binding, groove. The A pocket, which usually accommodates the free N-terminus of a, bound peptide, is closed, and the peptide is shifted one residue, such, that the P1 side chain is lodged in the B pocket. The formyl group is, coordinated by His-9 and a bound water on the floor of the groove.
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H2-M3 is a class Ib MHC molecule of the mouse with a 10(4)-fold preference for binding N-formylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a formylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray crystallography. M3, refined at 2.1 A resolution, resembles class la MHC molecules in its overall structure, but differs in the peptide-binding groove. The A pocket, which usually accommodates the free N-terminus of a bound peptide, is closed, and the peptide is shifted one residue, such that the P1 side chain is lodged in the B pocket. The formyl group is coordinated by His-9 and a bound water on the floor of the groove.
==About this Structure==
==About this Structure==
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1MHC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with NAG and FOR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MHC OCA].
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1MHC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=FOR:'>FOR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHC OCA].
==Reference==
==Reference==
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[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
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[[Category: Lindahl, K.Fischer.]]
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[[Category: Lindahl, K Fischer.]]
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[[Category: Wang, C.R.]]
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[[Category: Wang, C R.]]
[[Category: FOR]]
[[Category: FOR]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: histocompatibility antigen/peptide]]
[[Category: histocompatibility antigen/peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:25:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:10 2008''

Revision as of 11:55, 21 February 2008


1mhc, resolution 2.1Å

Drag the structure with the mouse to rotate

MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION

Overview

H2-M3 is a class Ib MHC molecule of the mouse with a 10(4)-fold preference for binding N-formylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a formylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray crystallography. M3, refined at 2.1 A resolution, resembles class la MHC molecules in its overall structure, but differs in the peptide-binding groove. The A pocket, which usually accommodates the free N-terminus of a bound peptide, is closed, and the peptide is shifted one residue, such that the P1 side chain is lodged in the B pocket. The formyl group is coordinated by His-9 and a bound water on the floor of the groove.

About this Structure

1MHC is a Protein complex structure of sequences from Mus musculus and Rattus rattus with and as ligands. Full crystallographic information is available from OCA.

Reference

Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3., Wang CR, Castano AR, Peterson PA, Slaughter C, Lindahl KF, Deisenhofer J, Cell. 1995 Aug 25;82(4):655-64. PMID:7664344

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