1c9l: Difference between revisions
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'''PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN''' | {{Structure | ||
|PDB= 1c9l |SIZE=350|CAPTION= <scene name='initialview01'>1c9l</scene>, resolution 2.90Å | |||
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'''PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C9L is a [ | 1C9L is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10655490 10655490] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helical hairpin]] | [[Category: helical hairpin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:38 2008'' |
Revision as of 11:21, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
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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