1utc

From Proteopedia

(Difference between revisions)

Current revision

Clathrin terminal domain complexed with TLPWDLWTT

Structural highlights

1utc is a 4 chain structure with sequence from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CLH1_BOVIN Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Miele AE, Watson PJ, Evans PR, Traub LM, Owen DJ. Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller. Nat Struct Mol Biol. 2004 Mar;11(3):242-8. Epub 2004 Feb 15. PMID:14981508 doi:10.1038/nsmb736

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1utc"

@@ Line 3: / Line 3: @@
 <StructureSection load='1utc' size='340' side='right'caption='[[1utc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1utc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UTC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1utc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UTC FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b89|1b89]], [[1ky7|1ky7]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1utc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1utc OCA], [https://pdbe.org/1utc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1utc RCSB], [https://www.ebi.ac.uk/pdbsum/1utc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1utc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CLH1_BOVIN CLH1_BOVIN]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. [[https://www.uniprot.org/uniprot/AMPH_HUMAN AMPH_HUMAN]] May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.
+[https://www.uniprot.org/uniprot/CLH1_BOVIN CLH1_BOVIN] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Evans, P R]]
+[[Category: Evans PR]]
-[[Category: Miele, A E]]
+[[Category: Miele AE]]
-[[Category: Owen, D J]]
+[[Category: Owen DJ]]
-[[Category: Clathrin]]
-[[Category: Cytoskeleton]]
-[[Category: Endocytosis]]

1utc

From Proteopedia

Current revision

Clathrin terminal domain complexed with TLPWDLWTT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox