1bxx
From Proteopedia
(New page: 200px<br /><applet load="1bxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxx, resolution 2.7Å" /> '''MU2 ADAPTIN SUBUNIT (...) |
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| - | [[Image:1bxx.gif|left|200px]]<br /><applet load="1bxx" size=" | + | [[Image:1bxx.gif|left|200px]]<br /><applet load="1bxx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bxx, resolution 2.7Å" /> | caption="1bxx, resolution 2.7Å" /> | ||
'''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH TGN38 INTERNALIZATION PEPTIDE DYQRLN'''<br /> | '''MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH TGN38 INTERNALIZATION PEPTIDE DYQRLN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many cell surface proteins are marked for endocytosis by a cytoplasmic | + | Many cell surface proteins are marked for endocytosis by a cytoplasmic sequence motif, tyrosine-X-X-(hydrophobic residue), that is recognized by the mu2 subunit of AP2 adaptors. Crystal structures of the internalization signal binding domain of mu2 complexed with the internalization signal peptides of epidermal growth factor receptor and the trans-Golgi network protein TGN38 have been determined at 2.7 angstrom resolution. The signal peptides adopted an extended conformation rather than the expected tight turn. Specificity was conferred by hydrophobic pockets that bind the tyrosine and leucine in the peptide. In the crystal, the protein forms dimers that could increase the strength and specificity of binding to dimeric receptors. |
==About this Structure== | ==About this Structure== | ||
| - | 1BXX 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:// | + | 1BXX 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=1BXX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Evans, P | + | [[Category: Evans, P R.]] |
| - | [[Category: Owen, D | + | [[Category: Owen, D J.]] |
[[Category: adaptor]] | [[Category: adaptor]] | ||
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
[[Category: peptide complex]] | [[Category: peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:16 2008'' |
Revision as of 10:00, 21 February 2008
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MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH TGN38 INTERNALIZATION PEPTIDE DYQRLN
Overview
Many cell surface proteins are marked for endocytosis by a cytoplasmic sequence motif, tyrosine-X-X-(hydrophobic residue), that is recognized by the mu2 subunit of AP2 adaptors. Crystal structures of the internalization signal binding domain of mu2 complexed with the internalization signal peptides of epidermal growth factor receptor and the trans-Golgi network protein TGN38 have been determined at 2.7 angstrom resolution. The signal peptides adopted an extended conformation rather than the expected tight turn. Specificity was conferred by hydrophobic pockets that bind the tyrosine and leucine in the peptide. In the crystal, the protein forms dimers that could increase the strength and specificity of binding to dimeric receptors.
About this Structure
1BXX is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
A structural explanation for the recognition of tyrosine-based endocytotic signals., Owen DJ, Evans PR, Science. 1998 Nov 13;282(5392):1327-32. PMID:9812899
Page seeded by OCA on Thu Feb 21 12:00:16 2008
