1gyw

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(New page: 200px<br /><applet load="1gyw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gyw, resolution 2.40&Aring;" /> '''GAMMA-ADAPTIN APPEND...)
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[[Image:1gyw.jpg|left|200px]]<br /><applet load="1gyw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gyw.jpg|left|200px]]<br /><applet load="1gyw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gyw, resolution 2.40&Aring;" />
caption="1gyw, resolution 2.40&Aring;" />
'''GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1 A753D MUTANT'''<br />
'''GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1 A753D MUTANT'''<br />
==Overview==
==Overview==
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The AP1 complex is one of a family of heterotetrameric clathrin-adaptor, complexes involved in vesicular trafficking between the Golgi and, endosomes. The complex has two large subunits, gamma and beta1, which can, be divided into trunk, hinge, and appendage domains. The 1.8 A resolution, structure of the gamma appendage is presented. The binding site for the, known gamma appendage ligand gamma-synergin is mapped through creation of, point mutations designed on the basis of the structure. We also show that, Eps15, a protein believed to be involved in vesicle formation at the, plasma membrane, is also a ligand of gamma appendage and binds to the same, site as gamma-synergin. This observation explains the demonstrated, brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi, complex.
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The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into trunk, hinge, and appendage domains. The 1.8 A resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.
==About this Structure==
==About this Structure==
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1GYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GYW OCA].
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1GYW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYW OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Evans, P.R.]]
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[[Category: Evans, P R.]]
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[[Category: Kent, H.M.]]
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[[Category: Kent, H M.]]
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[[Category: Mcmahon, H.M.]]
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[[Category: Mcmahon, H M.]]
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[[Category: Miele, A.E.]]
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[[Category: Miele, A E.]]
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[[Category: Owen, D.J.]]
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[[Category: Owen, D J.]]
[[Category: CL]]
[[Category: CL]]
[[Category: adaptor]]
[[Category: adaptor]]
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[[Category: endocytosis]]
[[Category: endocytosis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:21:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:30 2008''

Revision as of 10:55, 21 February 2008


1gyw, resolution 2.40Å

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GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1 A753D MUTANT

Overview

The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into trunk, hinge, and appendage domains. The 1.8 A resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.

About this Structure

1GYW is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin., Kent HM, McMahon HT, Evans PR, Benmerah A, Owen DJ, Structure. 2002 Aug;10(8):1139-48. PMID:12176391

Page seeded by OCA on Thu Feb 21 12:55:30 2008

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