1qab: Difference between revisions

Line 1:

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

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

caption="1qab, resolution 3.20Å" />

'''The structure of human retinol binding protein with its carrier protein transthyretin reveals interaction with the carboxy terminus of RBP'''<br />

==Overview==

Whether ultimately utilized as retinoic acid, retinal, or retinol, vitamin, A is transported to the target cells as all-trans-retinol bound to, retinol-binding protein (RBP). Circulating in the plasma, RBP itself is, bound to transthyretin (TTR, previously referred to as thyroxine-binding, prealbumin). In vitro one tetramer of TTR can bind two molecules of, retinol-binding protein. However, the concentration of RBP in the plasma, is limiting, and the complex isolated from serum is composed of TTR and, RBP in a 1 to 1 stoichiometry. We report here the crystallographic, structure at 3.2 A of the protein-protein complex of human RBP and TTR., RBP binds at a 2-fold axis of symmetry in the TTR tetramer, and, consequently the recognition site itself has 2-fold symmetry: Four TTR, amino acids (Arg-21, Val-20, Leu-82, and Ile-84) are contributed by two, monomers. Amino acids Trp-67, Phe-96, and Leu-63 and -97 from RBP are, flanked by the symmetry-related side chains from TTR. In addition, the, structure reveals an interaction of the carboxy terminus of RBP at the, protein-protein recognition interface. This interaction, which involves, Leu-182 and Leu-183 of RBP, is consistent with the observation that, naturally occurring truncated forms of the protein are more readily, cleared from plasma than full-length RBP. Complex formation prevents, extensive loss of RBP through glomerular filtration, and the loss of, Leu-182 and Leu-183 would result in a decreased affinity of RBP for TTR.

Whether ultimately utilized as retinoic acid, retinal, or retinol, vitamin A is transported to the target cells as all-trans-retinol bound to retinol-binding protein (RBP). Circulating in the plasma, RBP itself is bound to transthyretin (TTR, previously referred to as thyroxine-binding prealbumin). In vitro one tetramer of TTR can bind two molecules of retinol-binding protein. However, the concentration of RBP in the plasma is limiting, and the complex isolated from serum is composed of TTR and RBP in a 1 to 1 stoichiometry. We report here the crystallographic structure at 3.2 A of the protein-protein complex of human RBP and TTR. RBP binds at a 2-fold axis of symmetry in the TTR tetramer, and consequently the recognition site itself has 2-fold symmetry: Four TTR amino acids (Arg-21, Val-20, Leu-82, and Ile-84) are contributed by two monomers. Amino acids Trp-67, Phe-96, and Leu-63 and -97 from RBP are flanked by the symmetry-related side chains from TTR. In addition, the structure reveals an interaction of the carboxy terminus of RBP at the protein-protein recognition interface. This interaction, which involves Leu-182 and Leu-183 of RBP, is consistent with the observation that naturally occurring truncated forms of the protein are more readily cleared from plasma than full-length RBP. Complex formation prevents extensive loss of RBP through glomerular filtration, and the loss of Leu-182 and Leu-183 would result in a decreased affinity of RBP for TTR.

==About this Structure==

1QAB 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 RTL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1QAB OCA].

1QAB 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=RTL:'>RTL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAB OCA].

==Reference==

Line 18:

[[Category: transthyretin]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 00:31:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:32 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1qab.gif|left|200px]]<br /><applet load="1qab" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qab.gif|left|200px]]<br /><applet load="1qab" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1qab, resolution 3.20&Aring;" />
 '''The structure of human retinol binding protein with its carrier protein transthyretin reveals interaction with the carboxy terminus of RBP'''<br />
 ==Overview==
-Whether ultimately utilized as retinoic acid, retinal, or retinol, vitamin, A is transported to the target cells as all-trans-retinol bound to, retinol-binding protein (RBP). Circulating in the plasma, RBP itself is, bound to transthyretin (TTR, previously referred to as thyroxine-binding, prealbumin). In vitro one tetramer of TTR can bind two molecules of, retinol-binding protein. However, the concentration of RBP in the plasma, is limiting, and the complex isolated from serum is composed of TTR and, RBP in a 1 to 1 stoichiometry. We report here the crystallographic, structure at 3.2 A of the protein-protein complex of human RBP and TTR., RBP binds at a 2-fold axis of symmetry in the TTR tetramer, and, consequently the recognition site itself has 2-fold symmetry: Four TTR, amino acids (Arg-21, Val-20, Leu-82, and Ile-84) are contributed by two, monomers. Amino acids Trp-67, Phe-96, and Leu-63 and -97 from RBP are, flanked by the symmetry-related side chains from TTR. In addition, the, structure reveals an interaction of the carboxy terminus of RBP at the, protein-protein recognition interface. This interaction, which involves, Leu-182 and Leu-183 of RBP, is consistent with the observation that, naturally occurring truncated forms of the protein are more readily, cleared from plasma than full-length RBP. Complex formation prevents, extensive loss of RBP through glomerular filtration, and the loss of, Leu-182 and Leu-183 would result in a decreased affinity of RBP for TTR.
+Whether ultimately utilized as retinoic acid, retinal, or retinol, vitamin A is transported to the target cells as all-trans-retinol bound to retinol-binding protein (RBP). Circulating in the plasma, RBP itself is bound to transthyretin (TTR, previously referred to as thyroxine-binding prealbumin). In vitro one tetramer of TTR can bind two molecules of retinol-binding protein. However, the concentration of RBP in the plasma is limiting, and the complex isolated from serum is composed of TTR and RBP in a 1 to 1 stoichiometry. We report here the crystallographic structure at 3.2 A of the protein-protein complex of human RBP and TTR. RBP binds at a 2-fold axis of symmetry in the TTR tetramer, and consequently the recognition site itself has 2-fold symmetry: Four TTR amino acids (Arg-21, Val-20, Leu-82, and Ile-84) are contributed by two monomers. Amino acids Trp-67, Phe-96, and Leu-63 and -97 from RBP are flanked by the symmetry-related side chains from TTR. In addition, the structure reveals an interaction of the carboxy terminus of RBP at the protein-protein recognition interface. This interaction, which involves Leu-182 and Leu-183 of RBP, is consistent with the observation that naturally occurring truncated forms of the protein are more readily cleared from plasma than full-length RBP. Complex formation prevents extensive loss of RBP through glomerular filtration, and the loss of Leu-182 and Leu-183 would result in a decreased affinity of RBP for TTR.
 ==About this Structure==
-QAB 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 RTL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QAB OCA].
+QAB 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=RTL:'>RTL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAB OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: transthyretin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:31:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:32 2008''