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1mi1

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Revision as of 06:52, 25 August 2021

Crystal Structure of the PH-BEACH Domain of Human Neurobeachin

Structural highlights

1mi1 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[NBEA_HUMAN] Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity).[UniProtKB:Q9EPN1]

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 BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures. Unexpectedly, the structure also reveals that the BEACH domain is in extensive association with a novel, weakly conserved pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong interactions, suggesting they may function as a single unit. Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners.

Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain.,Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Kronke M, Tong L EMBO J. 2002 Sep 16;21(18):4785-95. PMID:12234919^[1]

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

References

↑ Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Kronke M, Tong L. Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain. EMBO J. 2002 Sep 16;21(18):4785-95. PMID:12234919

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/1mi1"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mi1' size='340' side='right'caption='[[1mi1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mi1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MI1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mi1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MI1 FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1mi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi1 OCA], [http://pdbe.org/1mi1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mi1 RCSB], [http://www.ebi.ac.uk/pdbsum/1mi1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi1 ProSAT], [http://www.topsan.org/Proteins/NESGC/1mi1 TOPSAN]</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=1mi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi1 OCA], [https://pdbe.org/1mi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mi1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi1 ProSAT], [https://www.topsan.org/Proteins/NESGC/1mi1 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NBEA_HUMAN NBEA_HUMAN]] Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity).[UniProtKB:Q9EPN1]
+[[https://www.uniprot.org/uniprot/NBEA_HUMAN NBEA_HUMAN]] Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity).[UniProtKB:Q9EPN1]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1mi1

From Proteopedia

Revision as of 06:52, 25 August 2021

Crystal Structure of the PH-BEACH Domain of Human Neurobeachin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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