2g30: Difference between revisions

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New page: left|200px<br /> <applet load="2g30" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g30, resolution 1.600Å" /> '''beta appendage of ...
 
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[[Image:2g30.gif|left|200px]]<br />
[[Image:2g30.gif|left|200px]]<br /><applet load="2g30" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2g30" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2g30, resolution 1.600&Aring;" />
caption="2g30, resolution 1.600&Aring;" />
'''beta appendage of AP2 complexed with ARH peptide'''<br />
'''beta appendage of AP2 complexed with ARH peptide'''<br />


==Overview==
==Overview==
Clathrin-associated sorting proteins (CLASPs) expand the repertoire of, endocytic cargo sorted into clathrin-coated vesicles beyond the, transmembrane proteins that bind physically to the AP-2 adaptor. LDL and, GPCRs are internalized by ARH and beta-arrestin, respectively. We show, that these two CLASPs bind selectively to the AP-2 beta2 appendage, platform via an alpha-helical [DE](n)X(1-2)FXX[FL]XXXR motif, and that, this motif also occurs and is functional in the epsins. In beta-arrestin, this motif maintains the endocytosis-incompetent state by binding back on, the folded core of the protein in a beta strand conformation. Triggered, via a beta-arrestin/GPCR interaction, the motif must be displaced and must, undergo a strand to helix transition to enable the beta2 appendage binding, that drives GPCR-beta-arrestin complexes into clathrin coats. Another, interaction surface on the beta2 appendage sandwich is identified for, proteins such as eps15 and clathrin, suggesting a mechanism by which, clathrin displaces eps15 to lattice edges during assembly.
Clathrin-associated sorting proteins (CLASPs) expand the repertoire of endocytic cargo sorted into clathrin-coated vesicles beyond the transmembrane proteins that bind physically to the AP-2 adaptor. LDL and GPCRs are internalized by ARH and beta-arrestin, respectively. We show that these two CLASPs bind selectively to the AP-2 beta2 appendage platform via an alpha-helical [DE](n)X(1-2)FXX[FL]XXXR motif, and that this motif also occurs and is functional in the epsins. In beta-arrestin, this motif maintains the endocytosis-incompetent state by binding back on the folded core of the protein in a beta strand conformation. Triggered via a beta-arrestin/GPCR interaction, the motif must be displaced and must undergo a strand to helix transition to enable the beta2 appendage binding that drives GPCR-beta-arrestin complexes into clathrin coats. Another interaction surface on the beta2 appendage sandwich is identified for proteins such as eps15 and clathrin, suggesting a mechanism by which clathrin displaces eps15 to lattice edges during assembly.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2G30 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 2G30 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb88_1.html Clathrin]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G30 OCA].  
2G30 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 2G30 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb88_1.html Clathrin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G30 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Collins, B.M.]]
[[Category: Collins, B M.]]
[[Category: Edeling, M.A.]]
[[Category: Edeling, M A.]]
[[Category: Owen, D.J.]]
[[Category: Owen, D J.]]
[[Category: Traub, L.M.]]
[[Category: Traub, L M.]]
[[Category: adaptor]]
[[Category: adaptor]]
[[Category: alpha-helical arh peptide]]
[[Category: alpha-helical arh peptide]]
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[[Category: sandwich domain]]
[[Category: sandwich domain]]


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