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2nup

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Revision as of 08:42, 18 October 2017

Crystal Structure of the human Sec23a/24a heterodimer, complexed with the SNARE protein Sec22b

Structural highlights

2nup is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1m2v, 1ifq, 2nut
Gene:	SEC23A (HUMAN), SEC24A (HUMAN), SEC22B, SEC22L1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[SC23A_HUMAN] Defects in SEC23A are the cause of craniolenticulosutural dysplasia (CLSD) [MIM:607812]; also known as cranio-lenticulo-sutural dysplasia. CLSD is an autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.^[1]

Function

[SC23A_HUMAN] Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex. [SC22B_HUMAN] SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.^[2] [SC24A_HUMAN] Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.

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

The mechanism of cargo concentration into ER-derived vesicles involves interactions between the COPII vesicular coat complex and cargo transport signals--peptide sequences of 10-15 residues. The SNARE protein Sec22 contains a signal that binds the COPII subcomplex Sec23/24 and specifies its endoplasmic reticulum (ER) exit as an unassembled SNARE. The 200 kDa crystal structure of Sec22 bound to Sec23/24 reveals that the transport signal is a folded epitope rather than a conventional short peptide sequence. The NIE segment of the SNARE motif folds against the N-terminal longin domain, and this closed form of Sec22 binds at the Sec23/24 interface. Thus, COPII recognizes unassembled Sec22 via a folded epitope, whereas Sec22 assembly into SNARE complexes would mask the NIE segment. The concept of a conformational epitope as a transport signal suggests packaging mechanisms in which a coat is sensitive to the folded state of a cargo protein or the assembled state of a multiprotein complex.

The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope.,Mancias JD, Goldberg J Mol Cell. 2007 May 11;26(3):403-14. PMID:17499046^[3]

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

References

↑ Boyadjiev SA, Fromme JC, Ben J, Chong SS, Nauta C, Hur DJ, Zhang G, Hamamoto S, Schekman R, Ravazzola M, Orci L, Eyaid W. Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking. Nat Genet. 2006 Oct;38(10):1192-7. Epub 2006 Sep 17. PMID:16980979 doi:10.1038/ng1876
↑ Nakajima K, Hirose H, Taniguchi M, Kurashina H, Arasaki K, Nagahama M, Tani K, Yamamoto A, Tagaya M. Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion. EMBO J. 2004 Aug 18;23(16):3216-26. Epub 2004 Jul 22. PMID:15272311 doi:10.1038/sj.emboj.7600333
↑ Mancias JD, Goldberg J. The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope. Mol Cell. 2007 May 11;26(3):403-14. PMID:17499046 doi:10.1016/j.molcel.2007.03.017

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nup"

Categories: Human | Goldberg, J | Mancias, J D | Human copii sec23-24 complexed with sec22 | Protein transport

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the human Sec23a/24a heterodimer, complexed with the SNARE protein Sec22b==
 <StructureSection load='2nup' size='340' side='right' caption='[[2nup]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m2v|1m2v]], [[1ifq|1ifq]], [[2nut|2nut]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEC23A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SEC24A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SEC22B, SEC22L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2nup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nup OCA], [http://pdbe.org/2nup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nup RCSB], [http://www.ebi.ac.uk/pdbsum/2nup PDBsum]</span></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=2nup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nup OCA], [http://pdbe.org/2nup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nup RCSB], [http://www.ebi.ac.uk/pdbsum/2nup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nup ProSAT]</span></td></tr>
 </table>
 == Disease ==

2nup

From Proteopedia

Revision as of 08:42, 18 October 2017

Crystal Structure of the human Sec23a/24a heterodimer, complexed with the SNARE protein Sec22b

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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