1u38

From Proteopedia

(Difference between revisions)

Revision as of 09:35, 29 September 2021

Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains

Structural highlights

1u38 is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1u37, 1u39, 1u3b
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[APBA1_HUMAN] Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.

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

Members of the X11/Mint family of multidomain adaptor proteins are composed of a divergent N terminus, a conserved PTB domain and a pair of C-terminal PDZ domains. Many proteins can interact with the PDZ tandem of X11 proteins, although the mechanism of such interactions is unclear. Here we show that the highly conserved C-terminal tail of X11alpha folds back and inserts into the target-binding groove of the first PDZ domain. The binding of this tail occludes the binding of other target peptides. This autoinhibited conformation of X11 requires that the two PDZ domains and the entire C-terminal tail be covalently connected to form an integral structural unit. The autoinhibited conformation of the X11 PDZ tandem provides a mechanistic explanation for the unique target-binding properties of the protein and hints at potential regulatory mechanisms for the X11-target interactions.

Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem.,Long JF, Feng W, Wang R, Chan LN, Ip FC, Xia J, Ip NY, Zhang M Nat Struct Mol Biol. 2005 Aug;12(8):722-8. Epub 2005 Jul 10. PMID:16007100^[1]

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

References

↑ Long JF, Feng W, Wang R, Chan LN, Ip FC, Xia J, Ip NY, Zhang M. Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem. Nat Struct Mol Biol. 2005 Aug;12(8):722-8. Epub 2005 Jul 10. PMID:16007100 doi:http://dx.doi.org/10.1038/nsmb958

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u38"

@@ Line 3: / Line 3: @@
 <StructureSection load='1u38' size='340' side='right'caption='[[1u38]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u38]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U38 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U38 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u38]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U38 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u37|1u37]], [[1u39|1u39]], [[1u3b|1u3b]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u37|1u37]], [[1u39|1u39]], [[1u3b|1u3b]]</div></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=1u38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u38 OCA], [http://pdbe.org/1u38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u38 RCSB], [http://www.ebi.ac.uk/pdbsum/1u38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u38 ProSAT]</span></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=1u38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u38 OCA], [https://pdbe.org/1u38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u38 RCSB], [https://www.ebi.ac.uk/pdbsum/1u38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u38 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/APBA1_HUMAN APBA1_HUMAN]] Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.
+[[https://www.uniprot.org/uniprot/APBA1_HUMAN APBA1_HUMAN]] Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1u38

From Proteopedia

Revision as of 09:35, 29 September 2021

Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox