1gyu: Difference between revisions

Revision as of 13:55, 21 February 2008

GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1

OverviewOverview

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 StructureAbout this Structure

1GYU is a Single protein structure of sequence from Mus musculus. The following page contains interesting information on the relation of 1GYU with [Clathrin]. Full crystallographic information is available from OCA.

ReferenceReference

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 12:55:33 2008

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OCA

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Evans, P.R.]]
+[[Category: Evans, P R.]]
-[[Category: Kent, H.M.]]
+[[Category: Kent, H M.]]
-[[Category: Mcmahon, H.M.]]
+[[Category: Mcmahon, H M.]]
-[[Category: Owen, D.J.]]
+[[Category: Owen, D J.]]
 [[Category: adaptin]]
 [[Category: adaptor]]
@@ Line 24: / Line 24: @@
 [[Category: golgi]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:54:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:33 2008''