1pdr: Difference between revisions

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==Overview==

PDZ domains (also known as DHR domains or GLGF repeats) are approximately, 90-residue repeats found in a number of proteins implicated in ion-channel, and receptor clustering, and the linking of receptors to effector enzymes., PDZ domains are protein-recognition modules; some recognize proteins, containing the consensus carboxy-terminal tripeptide motif S/TXV with high, specificity. Other PDZ domains form homotypic dimers: the PDZ domain of, the neuronal enzyme nitric oxide synthase binds to the PDZ domain of, PSD-95, an interaction that has been implicated in its synaptic, association. Here we report the crystal structure of the third PDZ domain, of the human homologue of the Drosophila discs-large tumour-suppressor, gene product, DlgA. It consists of a five-stranded antiparallel, beta-barrel flanked by three alpha-helices. A groove runs over the surface, of the domain, ending in a conserved hydrophobic pocket and a buried, arginine; we suggest that this is the binding site for the C-terminal, peptide.

PDZ domains (also known as DHR domains or GLGF repeats) are approximately 90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes. PDZ domains are protein-recognition modules; some recognize proteins containing the consensus carboxy-terminal tripeptide motif S/TXV with high specificity. Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of PSD-95, an interaction that has been implicated in its synaptic association. Here we report the crystal structure of the third PDZ domain of the human homologue of the Drosophila discs-large tumour-suppressor gene product, DlgA. It consists of a five-stranded antiparallel beta-barrel flanked by three alpha-helices. A groove runs over the surface of the domain, ending in a conserved hydrophobic pocket and a buried arginine; we suggest that this is the binding site for the C-terminal peptide.

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Cabral, J.M.]]

[[Category: Cabral, J M.]]

[[Category: Liddington, R.]]

[[Category: repeat]]

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[[Category: signal transduction]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-PDZ domains (also known as DHR domains or GLGF repeats) are approximately, 90-residue repeats found in a number of proteins implicated in ion-channel, and receptor clustering, and the linking of receptors to effector enzymes., PDZ domains are protein-recognition modules; some recognize proteins, containing the consensus carboxy-terminal tripeptide motif S/TXV with high, specificity. Other PDZ domains form homotypic dimers: the PDZ domain of, the neuronal enzyme nitric oxide synthase binds to the PDZ domain of, PSD-95, an interaction that has been implicated in its synaptic, association. Here we report the crystal structure of the third PDZ domain, of the human homologue of the Drosophila discs-large tumour-suppressor, gene product, DlgA. It consists of a five-stranded antiparallel, beta-barrel flanked by three alpha-helices. A groove runs over the surface, of the domain, ending in a conserved hydrophobic pocket and a buried, arginine; we suggest that this is the binding site for the C-terminal, peptide.
+PDZ domains (also known as DHR domains or GLGF repeats) are approximately 90-residue repeats found in a number of proteins implicated in ion-channel and receptor clustering, and the linking of receptors to effector enzymes. PDZ domains are protein-recognition modules; some recognize proteins containing the consensus carboxy-terminal tripeptide motif S/TXV with high specificity. Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of PSD-95, an interaction that has been implicated in its synaptic association. Here we report the crystal structure of the third PDZ domain of the human homologue of the Drosophila discs-large tumour-suppressor gene product, DlgA. It consists of a five-stranded antiparallel beta-barrel flanked by three alpha-helices. A groove runs over the surface of the domain, ending in a conserved hydrophobic pocket and a buried arginine; we suggest that this is the binding site for the C-terminal peptide.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Cabral, J.M.]]
+[[Category: Cabral, J M.]]
 [[Category: Liddington, R.]]
 [[Category: repeat]]
@@ Line 19: / Line 19: @@
 [[Category: signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:39:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:45 2008''