1utc: Difference between revisions
New page: left|200px<br /> <applet load="1utc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1utc, resolution 2.30Å" /> '''CLATHRIN TERMINAL D... |
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[[Image:1utc.gif|left|200px]]<br /> | [[Image:1utc.gif|left|200px]]<br /><applet load="1utc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1utc, resolution 2.30Å" /> | caption="1utc, resolution 2.30Å" /> | ||
'''CLATHRIN TERMINAL DOMAIN COMPLEXED WITH TLPWDLWTT'''<br /> | '''CLATHRIN TERMINAL DOMAIN COMPLEXED WITH TLPWDLWTT'''<br /> | ||
==Overview== | ==Overview== | ||
During the assembly of clathrin-coated vesicles, many peripheral membrane | During the assembly of clathrin-coated vesicles, many peripheral membrane proteins, including the amphiphysins, use LLDLD-type clathrin-box motifs to interact with the N-terminal beta-propeller domain (TD) of clathrin. The 2.3 A-resolution structure of the clathrin TD in complex with a TLPWDLWTT peptide from amphiphysin 1 delineates a second clathrin-binding motif, PWXXW (the W box), that binds at a site on the TD remote from the clathrin box-binding site. The presence of both sequence motifs within the unstructured region of the amphiphysins allows them to bind more tightly to free TDs than do other endocytic proteins that contain only clathrin-box motifs. This property, along with the propensity of the N-terminal BAR domain to bind curved membranes, will preferentially localize amphiphysin and its partner, dynamin, to the periphery of invaginated clathrin lattices. | ||
==Disease== | |||
Known disease associated with this structure: Myopathy, centronuclear, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601248 601248]] | |||
==About this Structure== | ==About this Structure== | ||
1UTC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | 1UTC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Evans, P | [[Category: Evans, P R.]] | ||
[[Category: Miele, A | [[Category: Miele, A E.]] | ||
[[Category: Owen, D | [[Category: Owen, D J.]] | ||
[[Category: clathrin]] | [[Category: clathrin]] | ||
[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:06 2008'' | ||
Revision as of 16:28, 21 February 2008
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CLATHRIN TERMINAL DOMAIN COMPLEXED WITH TLPWDLWTT
OverviewOverview
During the assembly of clathrin-coated vesicles, many peripheral membrane proteins, including the amphiphysins, use LLDLD-type clathrin-box motifs to interact with the N-terminal beta-propeller domain (TD) of clathrin. The 2.3 A-resolution structure of the clathrin TD in complex with a TLPWDLWTT peptide from amphiphysin 1 delineates a second clathrin-binding motif, PWXXW (the W box), that binds at a site on the TD remote from the clathrin box-binding site. The presence of both sequence motifs within the unstructured region of the amphiphysins allows them to bind more tightly to free TDs than do other endocytic proteins that contain only clathrin-box motifs. This property, along with the propensity of the N-terminal BAR domain to bind curved membranes, will preferentially localize amphiphysin and its partner, dynamin, to the periphery of invaginated clathrin lattices.
DiseaseDisease
Known disease associated with this structure: Myopathy, centronuclear, autosomal recessive OMIM:[601248]
About this StructureAbout this Structure
1UTC is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller., Miele AE, Watson PJ, Evans PR, Traub LM, Owen DJ, Nat Struct Mol Biol. 2004 Mar;11(3):242-8. Epub 2004 Feb 15. PMID:14981508
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