1o3x: Difference between revisions

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==Overview==

GGAs are critical for trafficking soluble proteins from the trans-Golgi, network (TGN) to endosomes/lysosomes through interactions with TGN-sorting, receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to, TGN membranes recruits its effector GGA by binding to the GAT domain, thus, facilitating recognition of GGA for cargo-loaded receptors. Here we report, the X-ray crystal structures of the human GGA1-GAT domain and the complex, between ARF1-GTP and the N-terminal region of the GAT domain. When, unbound, the GAT domain forms an elongated bundle of three a-helices with, a hydrophobic core. Structurally, this domain, combined with the preceding, VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In, the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of, GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a, hydrophobic manner. These data reveal a molecular mechanism underlying, membrane recruitment of adaptor proteins by ARF-GTP.

GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP.

==About this Structure==

1O3X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure ~~superseeds~~ the now removed PDB entry 1J2H. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O3X OCA].

1O3X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1J2H. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O3X OCA].

==Reference==

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[[Category: protein transport]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:32:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:13:05 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-GGAs are critical for trafficking soluble proteins from the trans-Golgi, network (TGN) to endosomes/lysosomes through interactions with TGN-sorting, receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to, TGN membranes recruits its effector GGA by binding to the GAT domain, thus, facilitating recognition of GGA for cargo-loaded receptors. Here we report, the X-ray crystal structures of the human GGA1-GAT domain and the complex, between ARF1-GTP and the N-terminal region of the GAT domain. When, unbound, the GAT domain forms an elongated bundle of three a-helices with, a hydrophobic core. Structurally, this domain, combined with the preceding, VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In, the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of, GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a, hydrophobic manner. These data reveal a molecular mechanism underlying, membrane recruitment of adaptor proteins by ARF-GTP.
+GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP.
 ==About this Structure==
-O3X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 1J2H. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O3X OCA].
+O3X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1J2H. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O3X OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: protein transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:32:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:13:05 2008''