1a1m: Difference between revisions

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[[Image:1a1m.~~gif~~|left|200px]]

[[Image:1a1m.png|left|200px]]

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~~'''~~MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2~~'''~~

===MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2===

~~==Overview==~~

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The ~~structure of~~ the ~~human MHC class I molecule HLA-B53 complexed~~ to ~~two nonameric peptide epitopes~~ (~~from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography~~ at 2.~~3 angstrom resolution~~. ~~The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles~~, ~~the B53 peptide-binding groove~~ is ~~widened by a significant (up to 1.25 angstrom) shift in~~ the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes.

The line below this paragraph, {{ABSTRACT_PUBMED_8624812}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8624812 is the PubMed ID number.

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==About this Structure==

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[[Category: Major histocompatibility antigen]]

[[Category: Mhc]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 09~~:40:18 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:47:47 2008''

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-[[Image:1a1m.gif|left|200px]]
+{{Seed}}
+[[Image:1a1m.png|left|200px]]
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 {{STRUCTURE_1a1m|  PDB=1a1m  |  SCENE=  }}
-'''MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2'''
+===MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2===
-==Overview==
+<!--
-The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes.
+The line below this paragraph, {{ABSTRACT_PUBMED_8624812}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8624812 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8624812}}
 ==About this Structure==
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 [[Category: Major histocompatibility antigen]]
 [[Category: Mhc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:40:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:47:47 2008''