1r5i: Difference between revisions

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[[Image:1r5i.~~gif~~|left|200px]]

[[Image:1r5i.png|left|200px]]

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~~'''~~Crystal structure of the MAM-MHC complex~~'''~~

===Crystal structure of the MAM-MHC complex===

~~==Overview==~~

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Mycoplasma arthritidis-derived mitogen (MAM) is a superantigen that can activate large fractions of T cells bearing particular TCR Vbeta elements. Here we report the crystal structure of MAM complexed with a major histocompatibility complex (MHC) antigen, HLA-~~DR1, loaded with haemagglutinin peptide 306~~-~~318 (HA).~~ The ~~structure reveals that MAM has a novel fold composed of two alpha-helical domains. This fold is entirely different from that of the pyrogenic superantigens~~, ~~consisting of a beta-grasped motif and a beta barrel. In the complex~~, the ~~N-terminal domain of MAM binds orthogonally~~ to the ~~MHC alpha1 domain and the bound HA peptide~~, ~~and to a lesser extent to~~ the ~~MHC beta1 domain~~. ~~Two MAM molecules form an asymmetric dimer and cross~~-~~link two MHC antigens to form a plausible, dimerized MAM~~-~~MHC complex. These data provide the first crystallographic evidence that superantigens can dimerize MHC molecules. Based on our structure, a model of the TCR2MAM2MHC2 complex is proposed.~~

The line below this paragraph, {{ABSTRACT_PUBMED_14962388}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14962388 is the PubMed ID number.

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==About this Structure==

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[[Category: Mhc]]

[[Category: Superantigen]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 07~~:06:23 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:05:39 2008''

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-[[Image:1r5i.gif|left|200px]]
+{{Seed}}
+[[Image:1r5i.png|left|200px]]
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 {{STRUCTURE_1r5i|  PDB=1r5i  |  SCENE=  }}
-'''Crystal structure of the MAM-MHC complex'''
+===Crystal structure of the MAM-MHC complex===
-==Overview==
+<!--
-Mycoplasma arthritidis-derived mitogen (MAM) is a superantigen that can activate large fractions of T cells bearing particular TCR Vbeta elements. Here we report the crystal structure of MAM complexed with a major histocompatibility complex (MHC) antigen, HLA-DR1, loaded with haemagglutinin peptide 306-318 (HA). The structure reveals that MAM has a novel fold composed of two alpha-helical domains. This fold is entirely different from that of the pyrogenic superantigens, consisting of a beta-grasped motif and a beta barrel. In the complex, the N-terminal domain of MAM binds orthogonally to the MHC alpha1 domain and the bound HA peptide, and to a lesser extent to the MHC beta1 domain. Two MAM molecules form an asymmetric dimer and cross-link two MHC antigens to form a plausible, dimerized MAM-MHC complex. These data provide the first crystallographic evidence that superantigens can dimerize MHC molecules. Based on our structure, a model of the TCR2MAM2MHC2 complex is proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_14962388}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14962388 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14962388}}
 ==About this Structure==
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 [[Category: Mhc]]
 [[Category: Superantigen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:06:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:05:39 2008''