1kjv: Difference between revisions

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[[Image:1kjv.jpg|left|200px]]<br /><applet load="1kjv" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

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

caption="1kjv, resolution 1.48Å" />

'''TAP-B-associated rat MHC class I molecule'''<br />

==Overview==

Antigenic peptides are loaded onto class I MHC molecules in the, endoplasmic reticulum (ER) by a complex consisting of the MHC class I, heavy chain, beta(2)-microglobulin, calreticulin, tapasin, Erp57 (ER60), and the transporter associated with antigen processing (TAP). While most, mammalian species transport these peptides into the ER via a single allele, of TAP, rats have evolved different TAPs, TAP-A and TAP-B, that are, present in different inbred strains. Each TAP delivers a different, spectrum of peptides and is associated genetically with distinct subsets, of MHC class Ia alleles, but the molecular basis for the conservation (or, co-evolution) of the two transporter alleles is unknown. We have, determined the crystal structures of a representative of each MHC subset, viz RT1-A(a) and RT1-A1(c), in association with high-affinity nonamer, peptides. The structures reveal how the chemical properties of the two, different rat MHC F-pockets match those of the corresponding C termini of, the peptides, corroborating biochemical data on the rates of peptide-MHC, complex assembly. An unusual sequence in RT1-A1(c) leads to a major, deviation from the highly conserved beta(3)/alpha(1) loop (residues 40-59), conformation in mouse and human MHC class I structures. This loop change, contributes to profound changes in the shape of the A-pocket in the, peptide-binding groove and may explain the function of RT1-A1(c) as an, inhibitory natural killer cell ligand.

Antigenic peptides are loaded onto class I MHC molecules in the endoplasmic reticulum (ER) by a complex consisting of the MHC class I heavy chain, beta(2)-microglobulin, calreticulin, tapasin, Erp57 (ER60) and the transporter associated with antigen processing (TAP). While most mammalian species transport these peptides into the ER via a single allele of TAP, rats have evolved different TAPs, TAP-A and TAP-B, that are present in different inbred strains. Each TAP delivers a different spectrum of peptides and is associated genetically with distinct subsets of MHC class Ia alleles, but the molecular basis for the conservation (or co-evolution) of the two transporter alleles is unknown. We have determined the crystal structures of a representative of each MHC subset, viz RT1-A(a) and RT1-A1(c), in association with high-affinity nonamer peptides. The structures reveal how the chemical properties of the two different rat MHC F-pockets match those of the corresponding C termini of the peptides, corroborating biochemical data on the rates of peptide-MHC complex assembly. An unusual sequence in RT1-A1(c) leads to a major deviation from the highly conserved beta(3)/alpha(1) loop (residues 40-59) conformation in mouse and human MHC class I structures. This loop change contributes to profound changes in the shape of the A-pocket in the peptide-binding groove and may explain the function of RT1-A1(c) as an inhibitory natural killer cell ligand.

==About this Structure==

1KJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KJV OCA].

1KJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJV OCA].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Rattus norvegicus]]

[[Category: Butcher, G.W.]]

[[Category: Butcher, G W.]]

[[Category: Joly, E.]]

[[Category: Rudolph, M.G.]]

[[Category: Rudolph, M G.]]

[[Category: Speir, J.A.]]

[[Category: Speir, J A.]]

[[Category: Stevens, J.]]

[[Category: Trowsdale, J.]]

[[Category: Wilson, I.A.]]

[[Category: Wilson, I A.]]

[[Category: SO4]]

[[Category: major histocompatibility complex]]

[[Category: peptide-mhc]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 19~~:18:~~06 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:54 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1kjv.jpg|left|200px]]<br /><applet load="1kjv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kjv.jpg|left|200px]]<br /><applet load="1kjv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kjv, resolution 1.48&Aring;" />
 '''TAP-B-associated rat MHC class I molecule'''<br />
 ==Overview==
-Antigenic peptides are loaded onto class I MHC molecules in the, endoplasmic reticulum (ER) by a complex consisting of the MHC class I, heavy chain, beta(2)-microglobulin, calreticulin, tapasin, Erp57 (ER60), and the transporter associated with antigen processing (TAP). While most, mammalian species transport these peptides into the ER via a single allele, of TAP, rats have evolved different TAPs, TAP-A and TAP-B, that are, present in different inbred strains. Each TAP delivers a different, spectrum of peptides and is associated genetically with distinct subsets, of MHC class Ia alleles, but the molecular basis for the conservation (or, co-evolution) of the two transporter alleles is unknown. We have, determined the crystal structures of a representative of each MHC subset, viz RT1-A(a) and RT1-A1(c), in association with high-affinity nonamer, peptides. The structures reveal how the chemical properties of the two, different rat MHC F-pockets match those of the corresponding C termini of, the peptides, corroborating biochemical data on the rates of peptide-MHC, complex assembly. An unusual sequence in RT1-A1(c) leads to a major, deviation from the highly conserved beta(3)/alpha(1) loop (residues 40-59), conformation in mouse and human MHC class I structures. This loop change, contributes to profound changes in the shape of the A-pocket in the, peptide-binding groove and may explain the function of RT1-A1(c) as an, inhibitory natural killer cell ligand.
+Antigenic peptides are loaded onto class I MHC molecules in the endoplasmic reticulum (ER) by a complex consisting of the MHC class I heavy chain, beta(2)-microglobulin, calreticulin, tapasin, Erp57 (ER60) and the transporter associated with antigen processing (TAP). While most mammalian species transport these peptides into the ER via a single allele of TAP, rats have evolved different TAPs, TAP-A and TAP-B, that are present in different inbred strains. Each TAP delivers a different spectrum of peptides and is associated genetically with distinct subsets of MHC class Ia alleles, but the molecular basis for the conservation (or co-evolution) of the two transporter alleles is unknown. We have determined the crystal structures of a representative of each MHC subset, viz RT1-A(a) and RT1-A1(c), in association with high-affinity nonamer peptides. The structures reveal how the chemical properties of the two different rat MHC F-pockets match those of the corresponding C termini of the peptides, corroborating biochemical data on the rates of peptide-MHC complex assembly. An unusual sequence in RT1-A1(c) leads to a major deviation from the highly conserved beta(3)/alpha(1) loop (residues 40-59) conformation in mouse and human MHC class I structures. This loop change contributes to profound changes in the shape of the A-pocket in the peptide-binding groove and may explain the function of RT1-A1(c) as an inhibitory natural killer cell ligand.
 ==About this Structure==
-KJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KJV OCA].
+KJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJV OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Butcher, G.W.]]
+[[Category: Butcher, G W.]]
 [[Category: Joly, E.]]
-[[Category: Rudolph, M.G.]]
+[[Category: Rudolph, M G.]]
-[[Category: Speir, J.A.]]
+[[Category: Speir, J A.]]
 [[Category: Stevens, J.]]
 [[Category: Trowsdale, J.]]
-[[Category: Wilson, I.A.]]
+[[Category: Wilson, I A.]]
 [[Category: SO4]]
 [[Category: major histocompatibility complex]]
 [[Category: peptide-mhc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:18:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:54 2008''