1dlh: Difference between revisions

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New page: left|200px<br /> <applet load="1dlh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dlh, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1dlh.gif|left|200px]]<br />
[[Image:1dlh.gif|left|200px]]<br /><applet load="1dlh" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1dlh" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1dlh, resolution 2.8&Aring;" />
caption="1dlh, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE'''<br />
'''CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE'''<br />


==Overview==
==Overview==
An influenza virus peptide binds to HLA-DR1 in an extended conformation, with a pronounced twist. Thirty-five per cent of the peptide surface is, accessible to solvent and potentially available for interaction with the, antigen receptor on T cells. Pockets in the peptide-binding site, accommodate five of the thirteen side chains of the bound peptide, and, explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between, conserved HLA-DR1 residues and the main chain of the peptide provide a, universal mode of peptide binding, distinct from the strategy used by, class I histocompatibility proteins.
An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.


==About this Structure==
==About this Structure==
1DLH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NAG and NDG as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1DLH with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb62_1.html Major Histocompatibility Complex]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DLH OCA].  
1DLH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1DLH with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb62_1.html Major Histocompatibility Complex]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLH OCA].  


==Reference==
==Reference==
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[[Category: Major Histocompatibility Complex]]
[[Category: Major Histocompatibility Complex]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Stern, L.J.]]
[[Category: Stern, L J.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: NDG]]
[[Category: NDG]]
[[Category: histocompatibility antigen]]
[[Category: histocompatibility antigen]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:33:38 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:49 2008''

Revision as of 13:17, 21 February 2008

File:1dlh.gif


1dlh, resolution 2.8Å

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CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE

OverviewOverview

An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.

About this StructureAbout this Structure

1DLH is a Protein complex structure of sequences from [1] with and as ligands. The following page contains interesting information on the relation of 1DLH with [Major Histocompatibility Complex]. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide., Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC, Nature. 1994 Mar 17;368(6468):215-21. PMID:8145819

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