1jf1: Difference between revisions

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New page: left|200px<br /> <applet load="1jf1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jf1, resolution 1.85Å" /> '''Crystal structure o...
 
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[[Image:1jf1.gif|left|200px]]<br />
[[Image:1jf1.gif|left|200px]]<br /><applet load="1jf1" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1jf1" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1jf1, resolution 1.85&Aring;" />
caption="1jf1, resolution 1.85&Aring;" />
'''Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A'''<br />
'''Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A'''<br />


==Overview==
==Overview==
We have determined high-resolution crystal structures of the complexes of, HLA-A2 molecules with two modified immunodominant peptides from the, melanoma tumor-associated protein Melan-A/Melanoma Ag recognized by T, cells-1. The two peptides, a decamer and nonamer with overlapping, sequences (ELAGIGILTV and ALGIGILTV), are modified in the second residue, to increase their affinity for HLA-A2. The modified decamer is more, immunogenic than the natural peptide and a candidate for peptide-based, melanoma immunotherapy. The crystal structures at 1.8 and 2.15 A, resolution define the differences in binding modes of the modified, peptides, including different clusters of water molecules that appear to, stabilize the peptide-HLA interaction. The structures suggest both how the, wild-type peptides would bind and how three categories of cytotoxic T, lymphocytes with differing fine specificity might recognize the two, peptides.
We have determined high-resolution crystal structures of the complexes of HLA-A2 molecules with two modified immunodominant peptides from the melanoma tumor-associated protein Melan-A/Melanoma Ag recognized by T cells-1. The two peptides, a decamer and nonamer with overlapping sequences (ELAGIGILTV and ALGIGILTV), are modified in the second residue to increase their affinity for HLA-A2. The modified decamer is more immunogenic than the natural peptide and a candidate for peptide-based melanoma immunotherapy. The crystal structures at 1.8 and 2.15 A resolution define the differences in binding modes of the modified peptides, including different clusters of water molecules that appear to stabilize the peptide-HLA interaction. The structures suggest both how the wild-type peptides would bind and how three categories of cytotoxic T lymphocytes with differing fine specificity might recognize the two peptides.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1JF1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JF1 OCA].  
1JF1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JF1 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Cerottini, J.C.]]
[[Category: Cerottini, J C.]]
[[Category: Karplus, M.]]
[[Category: Karplus, M.]]
[[Category: Luescher, I.]]
[[Category: Luescher, I.]]
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[[Category: Romero, P.]]
[[Category: Romero, P.]]
[[Category: Sliz, P.]]
[[Category: Sliz, P.]]
[[Category: Wiley, D.C.]]
[[Category: Wiley, D C.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: class i]]
[[Category: class i]]
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[[Category: vaccination]]
[[Category: vaccination]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:40:18 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:55 2008''

Revision as of 14:21, 21 February 2008

File:1jf1.gif


1jf1, resolution 1.85Å

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Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A

OverviewOverview

We have determined high-resolution crystal structures of the complexes of HLA-A2 molecules with two modified immunodominant peptides from the melanoma tumor-associated protein Melan-A/Melanoma Ag recognized by T cells-1. The two peptides, a decamer and nonamer with overlapping sequences (ELAGIGILTV and ALGIGILTV), are modified in the second residue to increase their affinity for HLA-A2. The modified decamer is more immunogenic than the natural peptide and a candidate for peptide-based melanoma immunotherapy. The crystal structures at 1.8 and 2.15 A resolution define the differences in binding modes of the modified peptides, including different clusters of water molecules that appear to stabilize the peptide-HLA interaction. The structures suggest both how the wild-type peptides would bind and how three categories of cytotoxic T lymphocytes with differing fine specificity might recognize the two peptides.

DiseaseDisease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]

About this StructureAbout this Structure

1JF1 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes., Sliz P, Michielin O, Cerottini JC, Luescher I, Romero P, Karplus M, Wiley DC, J Immunol. 2001 Sep 15;167(6):3276-84. PMID:11544315

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