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PDBsum entry 1gyu
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Gamma-Adaptin appendage domain: structure and binding site for eps15 and gamma-Synergin.
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Authors
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H.M.Kent,
H.T.Mcmahon,
P.R.Evans,
A.Benmerah,
D.J.Owen.
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Ref.
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Structure, 2002,
10,
1139-1148.
[DOI no: ]
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PubMed id
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Abstract
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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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Figure 1.
Figure 1. Comparison of the Structures of the g and a
Appendages(A) Superposition of the Ca traces of g appendage
(purple) and a appendage N-terminal subdomain (green). The two
overlay with an rms deviation of 1.8 Å for 96 Ca atoms.(B)
Schematic representation of the g appendage domain. Point
mutations that abrogate binding to g-synergin and Eps15 are
shown in yellow in ball and stick representation. All protein
structure pictures were made using Aesop (M.E.M. Noble, personal
communication).(C) Schematic representation of the a appendage
domain. The N-terminal subdomain is in green and the C-terminal
subdomain in gold.(D) Structure-based sequence alignment of g
appendages from human, mouse, Arabidopsis, and smutfungus, mouse
g2-appendage, human GGA1 appendage, and the N-terminal subdomain
of the a appendage. The positions of b strands are marked by
arrows and a helices with rods (purple human g appendage and
green a appendage). Conserved residues are indicated by gray
shading and residues identical between the g and a appendages
are marked with an asterisk.(E) Ca trace of the g appendage in
stereo representation.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
1139-1148)
copyright 2002.
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