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5m5r

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Revision as of 11:02, 12 August 2020

Clathrin heavy chain N-terminal domain bound to beta2 adaptin clathrin box motif

Structural highlights

5m5r is a 3 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	CLTC (BOVIN)
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. [AP2B1_HUMAN] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Short peptide motifs in unstructured regions of clathrin-adaptor proteins recruit clathrin to membranes to facilitate post-Golgi membrane transport. Three consensus clathrin-binding peptide sequences have been identified and structural studies show that each binds distinct sites on the clathrin heavy chain N-terminal domain (NTD). A fourth binding site for adaptors on NTD has been functionally identified but not structurally characterised. We have solved high resolution structures of NTD bound to peptide motifs from the cellular clathrin adaptors beta2 adaptin and amphiphysin plus a putative viral clathrin adaptor, hepatitis D virus large antigen (HDAg-L). Surprisingly, with each peptide we observe simultaneous peptide binding at multiple sites on NTD and viral peptides binding to the same sites as cellular peptides. Peptides containing clathrin-box motifs (CBMs) with consensus sequence LPhixPhi[DE] bind at the 'arrestin box' on NTD, between beta-propeller blades 4 and 5, which had previously been thought to bind a distinct consensus sequence. Further, we structurally define the fourth peptide binding site on NTD, which we term the Royle box. In vitro binding assays show that clathrin is more readily captured by cellular CBMs than by HDAg-L, and site-directed mutagenesis confirms that multiple binding sites on NTD contribute to efficient capture by CBM peptides.

Cellular and viral peptides bind multiple sites on the N-terminal domain of clathrin.,Muenzner J, Traub LM, Kelly BT, Graham SC Traffic. 2016 Nov 3. doi: 10.1111/tra.12457. PMID:27813245^[5]

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

References

↑ Nakatsu F, Ohno H. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct Funct. 2003 Oct;28(5):419-29. PMID:14745134
↑ Owen DJ, Collins BM, Evans PR. Adaptors for clathrin coats: structure and function. Annu Rev Cell Dev Biol. 2004;20:153-91. PMID:15473838 doi:10.1146/annurev.cellbio.20.010403.104543
↑ Huang F, Khvorova A, Marshall W, Sorkin A. Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference. J Biol Chem. 2004 Apr 16;279(16):16657-61. Epub 2004 Feb 25. PMID:14985334 doi:10.1074/jbc.C400046200
↑ Lau AW, Chou MM. The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway. J Cell Sci. 2008 Dec 15;121(Pt 24):4008-17. doi: 10.1242/jcs.033522. Epub 2008, Nov 25. PMID:19033387 doi:10.1242/jcs.033522
↑ Muenzner J, Traub LM, Kelly BT, Graham SC. Cellular and viral peptides bind multiple sites on the N-terminal domain of clathrin. Traffic. 2016 Nov 3. doi: 10.1111/tra.12457. PMID:27813245 doi:http://dx.doi.org/10.1111/tra.12457

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5m5r"

@@ Line 1: / Line 1: @@
 ==Clathrin heavy chain N-terminal domain bound to beta2 adaptin clathrin box motif==
-<StructureSection load='5m5r' size='340' side='right' caption='[[5m5r]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
+<StructureSection load='5m5r' size='340' side='right'caption='[[5m5r]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5m5r]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M5R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5m5r]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M5R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M5R FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m5r OCA], [http://pdbe.org/5m5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m5r RCSB], [http://www.ebi.ac.uk/pdbsum/5m5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m5r ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5m5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m5r OCA], [http://pdbe.org/5m5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m5r RCSB], [http://www.ebi.ac.uk/pdbsum/5m5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m5r ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5m5r" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Clathrin 3D structures|Clathrin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Bovin]]
+[[Category: Large Structures]]
 [[Category: Graham, S C]]
 [[Category: Muenzner, J]]

5m5r

From Proteopedia

Revision as of 11:02, 12 August 2020

Clathrin heavy chain N-terminal domain bound to beta2 adaptin clathrin box motif

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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