1hoc: Difference between revisions

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New page: left|200px<br /><applet load="1hoc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hoc, resolution 2.4Å" /> '''THE THREE-DIMENSIONAL...
 
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caption="1hoc, resolution 2.4&Aring;" />
caption="1hoc, resolution 2.4&Aring;" />
'''THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION'''<br />
'''THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION'''<br />


==Overview==
==Overview==
Solution at 2.4 A resolution of the structure of H-2Db with the influenza, virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV, (RGY-VYQGL) structure allow description of the molecular details of MHC, class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be, presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that, causes a compensatory arch in the backbone of the peptide, exposing the, arch residues to TCR contact and requiring the peptide to be at least 9, residues. This ridge occurs in about 40% of the known murine D and L, allelic molecules, classifying them as a structural subgroup.
Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.


==About this Structure==
==About this Structure==
1HOC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HOC OCA].  
1HOC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOC OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sacchettini, J.C.]]
[[Category: Sacchettini, J C.]]
[[Category: Young, A.C.M.]]
[[Category: Young, A C.M.]]
[[Category: Zhang, W.]]
[[Category: Zhang, W.]]
[[Category: histocompatibility antigen]]
[[Category: histocompatibility antigen]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:14 2008''

Revision as of 14:03, 21 February 2008

File:1hoc.gif


1hoc, resolution 2.4Å

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THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION

OverviewOverview

Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.

About this StructureAbout this Structure

1HOC is a Protein complex structure of sequences from Influenza a virus and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection., Young AC, Zhang W, Sacchettini JC, Nathenson SG, Cell. 1994 Jan 14;76(1):39-50. PMID:7506996

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