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PDBsum entry 3edv

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protein metals Protein-protein interface(s) links
Structural protein PDB id
3edv
Jmol
Contents
Protein chains
322 a.a. *
Metals
_MG ×13
Waters ×699
* Residue conservation analysis
PDB id:
3edv
Name: Structural protein
Title: Crystal structure of repeats 14-16 of beta2-spectrin
Structure: Spectrin beta chain, brain 1. Chain: a, b. Fragment: spectrin repeats 14-16. Synonym: spectrin, non-erythroid beta chain 1, beta-ii spectrin, fodrin beta chain. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: sptbn1, sptb2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.95Å     R-factor:   0.195     R-free:   0.250
Authors: P.Michaely,D.R.Tomchick
Key ref:
L.Davis et al. (2009). Localization and structure of the ankyrin-binding site on beta2-spectrin. J Biol Chem, 284, 6982-6987. PubMed id: 19098307 DOI: 10.1074/jbc.M809245200
Date:
03-Sep-08     Release date:   20-Jan-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q01082  (SPTB2_HUMAN) -  Spectrin beta chain, non-erythrocytic 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2364 a.a.
322 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     spectrin   1 term 
  Biochemical function     structural constituent of cytoskeleton     2 terms  

 

 
DOI no: 10.1074/jbc.M809245200 J Biol Chem 284:6982-6987 (2009)
PubMed id: 19098307  
 
 
Localization and structure of the ankyrin-binding site on beta2-spectrin.
L.Davis, K.Abdi, M.Machius, C.Brautigam, D.R.Tomchick, V.Bennett, P.Michaely.
 
  ABSTRACT  
 
Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the beta-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human beta2-spectrin at 1.95 A resolution together with mutagenesis data identifying the binding surface for ankyrins on beta2-spectrin.
 
  Selected figure(s)  
 
Figure 2.
Representative electron density. Shown is the representative electron density near Tyr^1874 with the final model shown as sticks. Carbons are colored gray; nitrogens, blue; and oxygens, red. Waters are shown as red pluses. Electron density at 1σ is shown as a green wire network.
Figure 5.
Inter-repeat contacts control orientation between repeats. Shown are ribbon representations of the inter-repeat junctions between repeats 14/15 (A) and repeats 15/16 (B) of β[2]-spectrin and the inter-repeat junctions between repeats 15/16 (C) and repeats 16/17 (D) of α[2]-spectrin. Linkers are colored dark blue in β[2]-spectrin and orange in α[2]-spectrin. Terminal residues of the inter-repeat contacts are labeled and shown as sticks.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2009, 284, 6982-6987) copyright 2009.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21412925 Y.Song, C.Antoniou, A.Memic, B.K.Kay, and L.W.Fung (2011).
Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs.
  Protein Sci, 20, 867-879.  
20411297 A.Czogalla, and A.F.Sikorski (2010).
Do we already know how spectrin attracts ankyrin?
  Cell Mol Life Sci, 67, 2679-2683.  
20185116 B.Olshansky, M.Delmar, and G.F.Tomaselli (2010).
The year in arrhythmias--2009: part I.
  Heart Rhythm, 7, 417-426.  
20573981 G.H.Mazock, A.Das, C.Base, and R.R.Dubreuil (2010).
Transgene rescue identifies an essential function for Drosophila beta spectrin in the nervous system and a selective requirement for ankyrin-2-binding activity.
  Mol Biol Cell, 21, 2860-2868.  
20101027 J.J.Ipsaro, and A.Mondragón (2010).
Structural basis for spectrin recognition by ankyrin.
  Blood, 115, 4093-4101.
PDB codes: 3kbt 3kbu
20197550 J.J.Ipsaro, S.L.Harper, T.E.Messick, R.Marmorstein, A.Mondragón, and D.W.Speicher (2010).
Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.
  Blood, 115, 4843-4852.
PDB code: 3lbx
20079712 P.J.La-Borde, P.R.Stabach, I.Simonović, J.S.Morrow, and M.Simonović (2010).
Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of beta-spectrin.
  Biochem Biophys Res Commun, 392, 490-494.  
19538529 M.Maciag, D.Płochocka, A.Adamowicz-Salach, and B.Burzyńska (2009).
Novel beta-spectrin mutations in hereditary spherocytosis associated with decreased levels of mRNA.
  Br J Haematol, 146, 326-332.  
19478050 P.S.Low (2009).
Where spectrin snuggles with ankyrin.
  Blood, 113, 5372-5373.  
19840192 S.R.Cunha, and P.J.Mohler (2009).
Ankyrin protein networks in membrane formation and stabilization.
  J Cell Mol Med, 13, 4364-4376.  
  20457566 V.Bennett, and J.Healy (2009).
Membrane domains based on ankyrin and spectrin associated with cell-cell interactions.
  Cold Spring Harb Perspect Biol, 1, a003012.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.