1c9l: Difference between revisions

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New page: left|200px<br /><applet load="1c9l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9l, resolution 2.90Å" /> '''PEPTIDE-IN-GROOVE IN...
 
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[[Image:1c9l.jpg|left|200px]]<br /><applet load="1c9l" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1c9l.jpg|left|200px]]<br /><applet load="1c9l" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1c9l, resolution 2.90&Aring;" />
caption="1c9l, resolution 2.90&Aring;" />
'''PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN'''<br />
'''PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN'''<br />


==Overview==
==Overview==
The "WD40" domain is a widespread recognition module for linking partner, proteins in intracellular networks of signaling and sorting. The clathrin, amino-terminal domain, which directs incorporation of cargo into coated, pits, is a beta-propeller closely related in structure to WD40 modules., The crystallographically determined structures of complexes of the, clathrin-terminal domain with peptides derived from two different cargo, adaptors, beta-arrestin 2 and the beta-subunit of the AP-3 complex, reveal, strikingly similar peptide-in-groove interactions. The two peptides in our, structures contain related, five-residue motifs, which form the core of, their contact with clathrin. A number of other proteins involved in, endocytosis have similar "clathrin-box" motifs, and it therefore is likely, that they all bind the terminal domain in the same way. We propose that a, peptide-in-groove interaction is an important general mode by which, beta-propellers recognize specific target proteins.
The "WD40" domain is a widespread recognition module for linking partner proteins in intracellular networks of signaling and sorting. The clathrin amino-terminal domain, which directs incorporation of cargo into coated pits, is a beta-propeller closely related in structure to WD40 modules. The crystallographically determined structures of complexes of the clathrin-terminal domain with peptides derived from two different cargo adaptors, beta-arrestin 2 and the beta-subunit of the AP-3 complex, reveal strikingly similar peptide-in-groove interactions. The two peptides in our structures contain related, five-residue motifs, which form the core of their contact with clathrin. A number of other proteins involved in endocytosis have similar "clathrin-box" motifs, and it therefore is likely that they all bind the terminal domain in the same way. We propose that a peptide-in-groove interaction is an important general mode by which beta-propellers recognize specific target proteins.


==About this Structure==
==About this Structure==
1C9L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C9L OCA].  
1C9L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9L OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Haar, E.ter.]]
[[Category: Haar, E ter.]]
[[Category: Harrison, S.C.]]
[[Category: Harrison, S C.]]
[[Category: Kirchhausen, T.]]
[[Category: Kirchhausen, T.]]
[[Category: beta-propeller]]
[[Category: beta-propeller]]
[[Category: helical hairpin]]
[[Category: helical hairpin]]


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Revision as of 13:04, 21 February 2008

File:1c9l.jpg


1c9l, resolution 2.90Å

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PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN

OverviewOverview

The "WD40" domain is a widespread recognition module for linking partner proteins in intracellular networks of signaling and sorting. The clathrin amino-terminal domain, which directs incorporation of cargo into coated pits, is a beta-propeller closely related in structure to WD40 modules. The crystallographically determined structures of complexes of the clathrin-terminal domain with peptides derived from two different cargo adaptors, beta-arrestin 2 and the beta-subunit of the AP-3 complex, reveal strikingly similar peptide-in-groove interactions. The two peptides in our structures contain related, five-residue motifs, which form the core of their contact with clathrin. A number of other proteins involved in endocytosis have similar "clathrin-box" motifs, and it therefore is likely that they all bind the terminal domain in the same way. We propose that a peptide-in-groove interaction is an important general mode by which beta-propellers recognize specific target proteins.

About this StructureAbout this Structure

1C9L is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin., ter Haar E, Harrison SC, Kirchhausen T, Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1096-100. PMID:10655490

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