1ydp: Difference between revisions

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[[Image:1ydp.gif|left|200px]]<br />

[[Image:1ydp.gif|left|200px]]<br /><applet load="1ydp" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1ydp" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1ydp, resolution 1.9Å" />

'''1.9A crystal structure of HLA-G'''<br />

==Overview==

HLA-G is a nonclassical major histocompatibility complex class I (MHC-I), molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the, maternal immune response. HLA-G binds a limited repertoire of peptides and, interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2, and possibly with certain natural killer cell receptors. To gain further, insights into HLA-G function, we determined the 1.9-A structure of a, monomeric HLA-G complexed to a natural endogenous peptide ligand from, histone H2A (RIIPRHLQL). An extensive network of contacts between the, peptide and the antigen-binding cleft reveal a constrained mode of binding, reminiscent of the nonclassical HLA-E molecule, thereby providing a, structural basis for the limited peptide repertoire of HLA-G. The alpha3, domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory, receptors, is structurally distinct from the alpha3 domains of classical, MHC-I molecules, providing a rationale for the observed affinity, differences for these ligands. The structural data suggest a head-to-tail, mode of dimerization, mediated by an intermolecular disulfide bond, that, is consistent with the observation of HLA-G dimers on the cell surface.

HLA-G is a nonclassical major histocompatibility complex class I (MHC-I) molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the maternal immune response. HLA-G binds a limited repertoire of peptides and interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2 and possibly with certain natural killer cell receptors. To gain further insights into HLA-G function, we determined the 1.9-A structure of a monomeric HLA-G complexed to a natural endogenous peptide ligand from histone H2A (RIIPRHLQL). An extensive network of contacts between the peptide and the antigen-binding cleft reveal a constrained mode of binding reminiscent of the nonclassical HLA-E molecule, thereby providing a structural basis for the limited peptide repertoire of HLA-G. The alpha3 domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory receptors, is structurally distinct from the alpha3 domains of classical MHC-I molecules, providing a rationale for the observed affinity differences for these ligands. The structural data suggest a head-to-tail mode of dimerization, mediated by an intermolecular disulfide bond, that is consistent with the observation of HLA-G dimers on the cell surface.

==Disease==

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==About this Structure==

1YDP 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 CO and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA].

1YDP 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=CO:'>CO</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Brooks, A.G.]]

[[Category: Brooks, A G.]]

[[Category: Clements, C.S.]]

[[Category: Clements, C S.]]

[[Category: Dunstone, M.A.]]

[[Category: Dunstone, M A.]]

[[Category: Freed, K.]]

[[Category: Hoare, H.L.]]

[[Category: Hoare, H L.]]

[[Category: Kjer-nielsen, L.]]

[[Category: Kostenko, L.]]

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[[Category: immune system]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:18:~~38 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:19 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ydp.gif|left|200px]]<br />
+[[Image:1ydp.gif|left|200px]]<br /><applet load="1ydp" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ydp" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ydp, resolution 1.9&Aring;" />
 '''1.9A crystal structure of HLA-G'''<br />
 ==Overview==
-HLA-G is a nonclassical major histocompatibility complex class I (MHC-I), molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the, maternal immune response. HLA-G binds a limited repertoire of peptides and, interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2, and possibly with certain natural killer cell receptors. To gain further, insights into HLA-G function, we determined the 1.9-A structure of a, monomeric HLA-G complexed to a natural endogenous peptide ligand from, histone H2A (RIIPRHLQL). An extensive network of contacts between the, peptide and the antigen-binding cleft reveal a constrained mode of binding, reminiscent of the nonclassical HLA-E molecule, thereby providing a, structural basis for the limited peptide repertoire of HLA-G. The alpha3, domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory, receptors, is structurally distinct from the alpha3 domains of classical, MHC-I molecules, providing a rationale for the observed affinity, differences for these ligands. The structural data suggest a head-to-tail, mode of dimerization, mediated by an intermolecular disulfide bond, that, is consistent with the observation of HLA-G dimers on the cell surface.
+HLA-G is a nonclassical major histocompatibility complex class I (MHC-I) molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the maternal immune response. HLA-G binds a limited repertoire of peptides and interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2 and possibly with certain natural killer cell receptors. To gain further insights into HLA-G function, we determined the 1.9-A structure of a monomeric HLA-G complexed to a natural endogenous peptide ligand from histone H2A (RIIPRHLQL). An extensive network of contacts between the peptide and the antigen-binding cleft reveal a constrained mode of binding reminiscent of the nonclassical HLA-E molecule, thereby providing a structural basis for the limited peptide repertoire of HLA-G. The alpha3 domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory receptors, is structurally distinct from the alpha3 domains of classical MHC-I molecules, providing a rationale for the observed affinity differences for these ligands. The structural data suggest a head-to-tail mode of dimerization, mediated by an intermolecular disulfide bond, that is consistent with the observation of HLA-G dimers on the cell surface.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-YDP 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 CO and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA].
+YDP 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=CO:'>CO</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Brooks, A.G.]]
+[[Category: Brooks, A G.]]
-[[Category: Clements, C.S.]]
+[[Category: Clements, C S.]]
-[[Category: Dunstone, M.A.]]
+[[Category: Dunstone, M A.]]
 [[Category: Freed, K.]]
-[[Category: Hoare, H.L.]]
+[[Category: Hoare, H L.]]
 [[Category: Kjer-nielsen, L.]]
 [[Category: Kostenko, L.]]
@@ Line 31: / Line 30: @@
 [[Category: immune system]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:18:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:19 2008''