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2rnd

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Revision as of 07:13, 10 June 2020

Structure of the N-terminal BARpeptide in DPC micelles

Structural highlights

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

Disease

[BIN1_HUMAN] Defects in BIN1 are the cause of centronuclear myopathy type 2 (CNM2) [MIM:255200]. A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers.^[1]

Function

[BIN1_HUMAN] May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation.

Publication Abstract from PubMed

BAR domains (Bin/Amphiphysin/Rvs-homology) generate and sense membrane curvature by binding the negatively charged membrane to their positively charged concave surfaces. N-BAR domains contain an N-terminal extension (helix-0) predicted to form an amphipathic helix upon membrane binding. We determined the NMR structure and nano-to-picosecond dynamics of helix-0 of the human Bin1/Amphiphysin II BAR domain in SDS and DPC micelles. Molecular dynamic simulations of this 34 amino acid peptide revealed electrostatic and hydrophobic interactions with the detergent molecules, which induce helical structure formation from residues 8-10 towards the C-terminus. The orientation in the micelles was experimentally confirmed by backbone amide proton exchange. Both simulation and experiment indicate that the N-terminal region is disordered, and the peptide curves to adopt the micelle shape. Deletion of helix-0 reduces tubulation of liposomes by the BAR domain, whereas the helix-0 peptide itself was fusogenic. These findings support models for membrane curving by BAR domains, where helix-0 increases the binding affinity to the membrane and enhances curvature generation.

Structure and dynamics of Helix-0 of the N-BAR domain in Lipid Micelles and Bilayers.,Low C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J Biophys J. 2008 Jul 25. PMID:18658220^[2]

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

References

↑ Nicot AS, Toussaint A, Tosch V, Kretz C, Wallgren-Pettersson C, Iwarsson E, Kingston H, Garnier JM, Biancalana V, Oldfors A, Mandel JL, Laporte J. Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy. Nat Genet. 2007 Sep;39(9):1134-9. Epub 2007 Aug 5. PMID:17676042 doi:10.1038/ng2086
↑ Low C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. Structure and dynamics of Helix-0 of the N-BAR domain in Lipid Micelles and Bilayers. Biophys J. 2008 Jul 25. PMID:18658220 doi:http://dx.doi.org/biophysj.108.134155

1 Structural highlights
2 Disease
3 Function
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/2rnd"

@@ Line 1: / Line 1: @@
 ==Structure of the N-terminal BARpeptide in DPC micelles==
-<StructureSection load='2rnd' size='340' side='right' caption='[[2rnd]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2rnd' size='340' side='right'caption='[[2rnd]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rnd]] is a 1 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=2RND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RND FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rnd]] is a 1 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=2RND OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RND FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rmy|2rmy]]</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=2rnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rnd OCA], [http://pdbe.org/2rnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rnd RCSB], [http://www.ebi.ac.uk/pdbsum/2rnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rnd ProSAT]</span></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=2rnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rnd OCA], [http://pdbe.org/2rnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rnd RCSB], [http://www.ebi.ac.uk/pdbsum/2rnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rnd ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 25: / Line 25: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Balbach, J]]
 [[Category: Loew, C]]

2rnd

From Proteopedia

Revision as of 07:13, 10 June 2020

Structure of the N-terminal BARpeptide in DPC micelles

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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