spacer
spacer

PDBsum entry 2spc

Go to PDB code: 
protein Protein-protein interface(s) links
Cytoskeleton PDB id
2spc
Jmol
Contents
Protein chains
107 a.a. *
Waters ×156
* Residue conservation analysis
PDB id:
2spc
Name: Cytoskeleton
Title: Crystal structure of the repetitive segments of spectrin
Structure: Spectrin. Chain: a, b. Engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227
Biol. unit: Dimer (from PQS)
Resolution:
1.80Å     R-factor:   0.203    
Authors: Y.Yan,E.Winograd,A.Viel,T.Cronin,S.C.Harrison,D.Branton
Key ref: Y.Yan et al. (1993). Crystal structure of the repetitive segments of spectrin. Science, 262, 2027-2030. PubMed id: 8266097 DOI: 10.1126/science.8266097
Date:
01-Mar-94     Release date:   31-May-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P13395  (SPTCA_DROME) -  Spectrin alpha chain
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2415 a.a.
107 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1126/science.8266097 Science 262:2027-2030 (1993)
PubMed id: 8266097  
 
 
Crystal structure of the repetitive segments of spectrin.
Y.Yan, E.Winograd, A.Viel, T.Cronin, S.C.Harrison, D.Branton.
 
  ABSTRACT  
 
The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.
 

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.  
20668894 A.J.Baines (2010).
The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.
  Protoplasma, 244, 99.  
20833645 C.S.Clemen, K.Tangavelou, K.H.Strucksberg, S.Just, L.Gaertner, H.Regus-Leidig, M.Stumpf, J.Reimann, R.Coras, R.O.Morgan, M.P.Fernandez, A.Hofmann, S.Müller, B.Schoser, F.G.Hanisch, W.Rottbauer, I.Blümcke, S.von Hörsten, L.Eichinger, and R.Schröder (2010).
Strumpellin is a novel valosin-containing protein binding partner linking hereditary spastic paraplegia to protein aggregation diseases.
  Brain, 133, 2920-2941.  
20502633 G.B.Banks, L.M.Judge, J.M.Allen, and J.S.Chamberlain (2010).
The polyproline site in hinge 2 influences the functional capacity of truncated dystrophins.
  PLoS Genet, 6, e1000958.  
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
20399181 M.V.Airola, K.J.Watts, A.M.Bilwes, and B.R.Crane (2010).
Structure of concatenated HAMP domains provides a mechanism for signal transduction.
  Structure, 18, 436-448.
PDB code: 3lnr
19369950 A.G.Maier, B.M.Cooke, A.F.Cowman, and L.Tilley (2009).
Malaria parasite proteins that remodel the host erythrocyte.
  Nat Rev Microbiol, 7, 341-354.  
19445951 B.G.Wensley, M.Gärtner, W.X.Choo, S.Batey, and J.Clarke (2009).
Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanisms.
  J Mol Biol, 390, 1074-1085.  
19072330 Q.Li, and L.W.Fung (2009).
Structural and dynamic study of the tetramerization region of non-erythroid alpha-spectrin: a frayed helix revealed by site-directed spin labeling electron paramagnetic resonance.
  Biochemistry, 48, 206-215.  
18287096 A.Das, C.Base, D.Manna, W.Cho, and R.R.Dubreuil (2008).
Unexpected complexity in the mechanisms that target assembly of the spectrin cytoskeleton.
  J Biol Chem, 283, 12643-12653.  
18682224 T.Pavkov, E.M.Egelseer, M.Tesarz, D.I.Svergun, U.B.Sleytr, and W.Keller (2008).
The structure and binding behavior of the bacterial cell surface layer protein SbsC.
  Structure, 16, 1226-1237.
PDB code: 2ra1
18815288 X.An, E.Gauthier, X.Zhang, X.Guo, D.J.Anstee, N.Mohandas, and J.A.Chasis (2008).
Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin.
  Blood, 112, 5212-5218.  
17905835 F.Long, D.McElheny, S.Jiang, S.Park, M.S.Caffrey, and L.W.Fung (2007).
Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin.
  Protein Sci, 16, 2519-2530.  
17521916 L.W.Zilch, D.T.Kaleta, M.Kohtani, R.Krishnan, and M.F.Jarrold (2007).
Folding and unfolding of helix-turn-helix motifs in the gas phase.
  J Am Soc Mass Spectrom, 18, 1239-1248.  
17468340 X.Pei, X.Guo, R.Coppel, S.Bhattacharjee, K.Haldar, W.Gratzer, N.Mohandas, and X.An (2007).
The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion.
  Blood, 110, 1036-1042.  
17607528 Y.Oh, and L.W.Fung (2007).
Brain proteins interacting with the tetramerization region of non-erythroid alpha spectrin.
  Cell Mol Biol Lett, 12, 604-620.  
17060500 A.Das, C.Base, S.Dhulipala, and R.R.Dubreuil (2006).
Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway.
  J Cell Biol, 175, 325-335.  
16407147 M.Salomao, X.An, X.Guo, W.B.Gratzer, N.Mohandas, and A.J.Baines (2006).
Mammalian alpha I-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytes.
  Proc Natl Acad Sci U S A, 103, 643-648.  
17091212 R.R.Dubreuil (2006).
Functional links between membrane transport and the spectrin cytoskeleton.
  J Membr Biol, 211, 151-161.  
17108086 S.Batey, and J.Clarke (2006).
Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains.
  Proc Natl Acad Sci U S A, 103, 18113-18118.  
16387757 S.Batey, K.A.Scott, and J.Clarke (2006).
Complex folding kinetics of a multidomain protein.
  Biophys J, 90, 2120-2130.  
16891371 S.Paramore, and G.A.Voth (2006).
Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.
  Biophys J, 91, 3436-3445.  
16227506 S.Paramore, G.S.Ayton, D.T.Mirijanian, and G.A.Voth (2006).
Extending a spectrin repeat unit. I: linear force-extension response.
  Biophys J, 90, 92.  
16227505 S.Paramore, G.S.Ayton, and G.A.Voth (2006).
Extending a spectrin repeat unit. II: rupture behavior.
  Biophys J, 90, 101-111.  
16331985 C.M.Taylor, and A.E.Keating (2005).
Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain.
  Biochemistry, 44, 16246-16256.  
16237665 D.A.Starr, and J.A.Fischer (2005).
KASH 'n Karry: the KASH domain family of cargo-specific cytoskeletal adaptor proteins.
  Bioessays, 27, 1136-1146.  
16330710 K.Wilhelmsen, S.H.Litjens, I.Kuikman, N.Tshimbalanga, H.Janssen, I.van den Bout, K.Raymond, and A.Sonnenberg (2005).
Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin.
  J Cell Biol, 171, 799-810.  
15711878 S.Ray, M.Bhattacharyya, and A.Chakrabarti (2005).
Conformational study of spectrin in presence of submolar concentrations of denaturants.
  J Fluoresc, 15, 61-70.  
15062087 H.Kusunoki, R.I.MacDonald, and A.Mondragón (2004).
Structural insights into the stability and flexibility of unusual erythroid spectrin repeats.
  Structure, 12, 645-656.
PDB code: 1s35
14752198 J.Holton, and T.Alber (2004).
Automated protein crystal structure determination using ELVES.
  Proc Natl Acad Sci U S A, 101, 1537-1542.
PDB codes: 1rb1 1rb4 1rb5 1rb6 3k7z
14536023 M.Grynberg, L.Jaroszewski, and A.Godzik (2003).
Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization.
  BMC Bioinformatics, 4, 46.  
14661984 S.Mehboob, J.Jacob, M.May, L.Kotula, P.Thiyagarajan, M.E.Johnson, and L.W.Fung (2003).
Structural analysis of the alpha N-terminal region of erythroid and nonerythroid spectrins by small-angle X-ray scattering.
  Biochemistry, 42, 14702-14710.  
12451592 S.Ray, and A.Chakrabarti (2003).
Erythroid spectrin in miceller detergents.
  Cell Motil Cytoskeleton, 54, 16-28.  
12038451 B.H.Luo, S.Mehboob, M.G.Hurtuk, N.H.Pipalia, and L.W.Fung (2002).
Important region in the beta-spectrin C-terminus for spectrin tetramer formation.
  Eur J Haematol, 68, 73-79.  
12006649 I.N.Rybakova, J.R.Patel, K.E.Davies, P.D.Yurchenco, and J.M.Ervasti (2002).
Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle.
  Mol Biol Cell, 13, 1512-1521.  
12496130 M.Damelin, and P.A.Silver (2002).
In situ analysis of spatial relationships between proteins of the nuclear pore complex.
  Biophys J, 83, 3626-3636.  
12021428 Y.Liu, and D.Eisenberg (2002).
3D domain swapping: as domains continue to swap.
  Protein Sci, 11, 1285-1299.  
11169588 G.H.Thomas (2001).
Spectrin: the ghost in the machine.
  Bioessays, 23, 152-160.  
11566764 I.L.Jäger (2001).
The "sticky chain": a kinetic model for the deformation of biological macromolecules.
  Biophys J, 81, 1897-1906.  
11709166 J.W.O'Neill, D.E.Kim, K.Johnsen, D.Baker, and K.Y.Zhang (2001).
Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.
  Structure, 9, 1017-1027.
PDB codes: 1k50 1k51 1k52 1k53
11443637 S.Ranganathan, N.Menhart, N.Topouzian, and L.W.Fung (2001).
Laboratory method to study mutational effects on human erythrocyte spectrin tetramerization.
  Am J Hematol, 67, 247-251.  
10866978 L.Cherry, L.W.Fung, and N.Menhart (2000).
Flexibility of the alpha-spectrin N-terminus by EPR and fluorescence polarization.
  Biophys J, 79, 526-535.  
10785404 L.Galluzzi, G.Nicolas, M.Paiardini, M.Magnani, and M.C.Lecomte (2000).
Identification of ubiquitinated repeats in human erythroid alpha-spectrin.
  Eur J Biochem, 267, 2812-2819.  
10811832 M.Hammarlund, W.S.Davis, and E.M.Jorgensen (2000).
Mutations in beta-spectrin disrupt axon outgrowth and sarcomere structure.
  J Cell Biol, 149, 931-942.  
11086001 S.Berghs, D.Aggujaro, R.Dirkx, E.Maksimova, P.Stabach, J.M.Hermel, J.P.Zhang, W.Philbrick, V.Slepnev, T.Ort, and M.Solimena (2000).
betaIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system.
  J Cell Biol, 151, 985.  
10607557 A.McGough (1999).
How to build a molecular shock absorber.
  Curr Biol, 9, R887-R889.  
10625438 C.D.Cianci, Z.Zhang, D.Pradhan, and J.S.Morrow (1999).
Brain and muscle express a unique alternative transcript of alphaII spectrin.
  Biochemistry, 38, 15721-15730.  
10601340 C.L.Leung, D.Sun, M.Zheng, D.R.Knowles, and R.K.Liem (1999).
Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons.
  J Cell Biol, 147, 1275-1286.  
10477760 D.C.Zarnescu, and G.H.Thomas (1999).
Apical spectrin is essential for epithelial morphogenesis but not apicobasal polarity in Drosophila.
  J Cell Biol, 146, 1075-1086.  
9990286 M.Van Troys, J.Vandekerckhove, and C.Ampe (1999).
Structural modules in actin-binding proteins: towards a new classification.
  Biochim Biophys Acta, 1448, 323-348.  
10366671 P.J.O'Toole, C.Wolfe, S.Ladha, and R.J.Cherry (1999).
Rapid diffusion of spectrin bound to a lipid surface.
  Biochim Biophys Acta, 1419, 64-70.  
10090742 R.Peteranderl, M.Rabenstein, Y.K.Shin, C.W.Liu, D.E.Wemmer, D.S.King, and H.C.Nelson (1999).
Biochemical and biophysical characterization of the trimerization domain from the heat shock transcription factor.
  Biochemistry, 38, 3559-3569.  
9731771 A.J.Murray, J.G.Head, J.J.Barker, and R.L.Brady (1998).
Engineering an intertwined form of CD2 for stability and assembly.
  Nat Struct Biol, 5, 778-782.
PDB codes: 1a64 1a6p 1a7b
9631289 A.McGough (1998).
F-actin-binding proteins.
  Curr Opin Struct Biol, 8, 166-176.  
9671502 A.P.Saint-Jean, K.R.Phillips, D.J.Creighton, and M.J.Stone (1998).
Active monomeric and dimeric forms of Pseudomonas putida glyoxalase I: evidence for 3D domain swapping.
  Biochemistry, 37, 10345-10353.  
9843421 D.Lusitani, N.Menhart, T.A.Keiderling, and L.W.Fung (1998).
Ionic strength effect on the thermal unfolding of alpha-spectrin peptides.
  Biochemistry, 37, 16546-16554.  
9700162 F.Rivero, A.Kuspa, R.Brokamp, M.Matzner, and A.A.Noegel (1998).
Interaptin, an actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments.
  J Cell Biol, 142, 735-750.  
9565750 J.P.Schneider, A.Lombardi, and W.F.DeGrado (1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
  Fold Des, 3, R29-R40.  
9501083 P.Young, C.Ferguson, S.Bañuelos, and M.Gautel (1998).
Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin.
  EMBO J, 17, 1614-1624.  
9484592 Y.A.Puius, N.M.Mahoney, and S.C.Almo (1998).
The modular structure of actin-regulatory proteins.
  Curr Opin Cell Biol, 10, 23-34.  
  9568891 Y.Yan, Y.Li, S.Munshi, V.Sardana, J.L.Cole, M.Sardana, C.Steinkuehler, L.Tomei, R.De Francesco, L.C.Kuo, and Z.Chen (1998).
Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form.
  Protein Sci, 7, 837-847.
PDB codes: 1jxp 1ns3
9204281 A.Lupas (1997).
Predicting coiled-coil regions in proteins.
  Curr Opin Struct Biol, 7, 388-393.  
9067620 E.Kahana, G.Flood, and W.B.Gratzer (1997).
Physical properties of dystrophin rod domain.
  Cell Motil Cytoskeleton, 36, 246-252.  
9188694 G.E.Begg, M.B.Morris, and G.B.Ralston (1997).
Comparison of the salt-dependent self-association of brain and erythroid spectrin.
  Biochemistry, 36, 6977-6985.  
9129841 J.C.Hansen, R.Skalak, S.Chien, and A.Hoger (1997).
Influence of network topology on the elasticity of the red blood cell membrane skeleton.
  Biophys J, 72, 2369-2381.  
9094325 J.M.Squire (1997).
Architecture and function in the muscle sarcomere.
  Curr Opin Struct Biol, 7, 247-257.  
9297972 J.Pascual, J.Castresana, and M.Saraste (1997).
Evolution of the spectrin repeat.
  Bioessays, 19, 811-817.  
10904556 K.A.Bode, and J.Applequist (1997).
Helix bundles and coiled coils in alpha-spectrin and tropomyosin: a theoretical CD study.
  Biopolymers, 42, 855-860.  
9303002 K.V.Kishan, G.Scita, W.T.Wong, P.P.Di Fiore, and M.E.Newcomer (1997).
The SH3 domain of Eps8 exists as a novel intertwined dimer.
  Nat Struct Biol, 4, 739-743.
PDB code: 1aoj
  9007979 N.L.Ogihara, M.S.Weiss, W.F.Degrado, and D.Eisenberg (1997).
The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies.
  Protein Sci, 6, 80-88.
PDB code: 1coi
9118945 P.Fernandez-Silva, F.Martinez-Azorin, V.Micol, and G.Attardi (1997).
The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions.
  EMBO J, 16, 1066-1079.  
9164464 P.Fucini, C.Renner, C.Herberhold, A.A.Noegel, and T.A.Holak (1997).
The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.
  Nat Struct Biol, 4, 223-230.
PDB code: 1ksr
9005995 P.G.Gallagher, M.J.Petruzzi, S.A.Weed, Z.Zhang, S.L.Marchesi, N.Mohandas, J.S.Morrow, and B.G.Forget (1997).
Mutation of a highly conserved residue of betaI spectrin associated with fatal and near-fatal neonatal hemolytic anemia.
  J Clin Invest, 99, 267-277.  
8993318 P.R.Stabach, C.D.Cianci, S.B.Glantz, Z.Zhang, and J.S.Morrow (1997).
Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility.
  Biochemistry, 36, 57-65.  
9261069 P.Sliz, R.Engelmann, W.Hengstenberg, and E.F.Pai (1997).
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.
  Structure, 5, 775-788.
PDB code: 1e2a
9003183 S.E.Kurzawa, D.J.Manstein, and M.A.Geeves (1997).
Dictyostelium discoideum myosin II: characterization of functional myosin motor fragments.
  Biochemistry, 36, 317-323.  
9092829 T.M.DeSilva, S.L.Harper, L.Kotula, P.Hensley, P.J.Curtis, L.Otvos, and D.W.Speicher (1997).
Physical properties of a single-motif erythrocyte spectrin peptide: a highly stable independently folding unit.
  Biochemistry, 36, 3991-3997.  
9284287 Y.Sharf, T.Knubovets, D.Dayan, A.Hirshberg, S.Akselrod, and G.Navon (1997).
The source of NMR-detected motional anisotropy of water in blood vessel walls.
  Biophys J, 73, 1198-1204.  
9062072 A.Lombardi, J.W.Bryson, and W.F.DeGrado (1996).
De novo design of heterotrimeric coiled coils.
  Biopolymers, 40, 495-504.  
8791400 A.Viel, and D.Branton (1996).
Spectrin: on the path from structure to function.
  Curr Opin Cell Biol, 8, 49-55.  
8696076 E.F.Wenegieme, A.P.Naren, and J.A.Bobich (1996).
Cation effects on the conformations of muscle and non-muscle alpha-actinins.
  Biometals, 9, 259-265.  
8611512 G.Ralston, T.Cronin, and D.Branton (1996).
Self-association of spectrin's repeating segments.
  Biochemistry, 35, 5257-5263.  
8932827 H.Hassoun, and J.Palek (1996).
Hereditary spherocytosis: a review of the clinical and molecular aspects of the disease.
  Blood Rev, 10, 129-147.  
8866745 H.M.Sadoulet-Puccio, and L.M.Kunkel (1996).
Dystrophin and its isoforms.
  Brain Pathol, 6, 25-35.  
8770194 J.C.Hansen, R.Skalak, S.Chien, and A.Hoger (1996).
An elastic network model based on the structure of the red blood cell membrane skeleton.
  Biophys J, 70, 146-166.  
8752217 J.Faix, M.Steinmetz, H.Boves, R.A.Kammerer, F.Lottspeich, U.Mintert, J.Murphy, A.Stock, U.Aebi, and G.Gerisch (1996).
Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail.
  Cell, 86, 631-642.  
  8947029 M.Anson, M.A.Geeves, S.E.Kurzawa, and D.J.Manstein (1996).
Myosin motors with artificial lever arms.
  EMBO J, 15, 6069-6074.  
8874034 R.Calvert, E.Kahana, and W.B.Gratzer (1996).
Stability of the dystrophin rod domain fold: evidence for nested repeating units.
  Biophys J, 71, 1605-1610.  
8909548 S.M.Marfatia, J.H.Morais Cabral, L.Lin, C.Hough, P.J.Bryant, L.Stolz, and A.H.Chishti (1996).
Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton.
  J Cell Biol, 135, 753-766.  
  8520486 D.N.Woolfson, and T.Alber (1995).
Predicting oligomerization states of coiled coils.
  Protein Sci, 4, 1596-1607.  
7857651 G.L.Lyford, K.Yamagata, W.E.Kaufmann, C.A.Barnes, L.K.Sanders, N.G.Copeland, D.J.Gilbert, N.A.Jenkins, A.A.Lanahan, and P.F.Worley (1995).
Arc, a growth factor and activity-regulated gene, encodes a novel cytoskeleton-associated protein that is enriched in neuronal dendrites.
  Neuron, 14, 433-445.  
7851407 G.Travé, A.Pastore, M.Hyvönen, and M.Saraste (1995).
The C-terminal domain of alpha-spectrin is structurally related to calmodulin.
  Eur J Biochem, 227, 35-42.  
7822424 H.Deng, J.K.Lee, L.S.Goldstein, and D.Branton (1995).
Drosophila development requires spectrin network formation.
  J Cell Biol, 128, 71-79.  
8675627 H.Hassoun, J.N.Vassiliadis, J.Murray, S.J.Yi, M.Hanspal, R.E.Ware, S.S.Winter, S.S.Chiou, and J.Palek (1995).
Molecular basis of spectrin deficiency in beta spectrin Durham. A deletion within beta spectrin adjacent to the ankyrin-binding site precludes spectrin attachment to the membrane in hereditary spherocytosis.
  J Clin Invest, 96, 2623-2629.  
7612181 J.Delaunay (1995).
Genetic disorders of the red cell membrane.
  Crit Rev Oncol Hematol, 19, 79.  
  8580836 M.J.Bennett, M.P.Schlunegger, and D.Eisenberg (1995).
3D domain swapping: a mechanism for oligomer assembly.
  Protein Sci, 4, 2455-2468.  
7883966 P.G.Gallagher, S.A.Weed, W.T.Tse, L.Benoit, J.S.Morrow, S.L.Marchesi, N.Mohandas, and B.G.Forget (1995).
Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene.
  J Clin Invest, 95, 1174-1182.  
7925443 A.P.Gilmore, T.Parr, B.Patel, W.B.Gratzer, and D.R.Critchley (1994).
Analysis of the phasing of four spectrin-like repeats in alpha-actinin.
  Eur J Biochem, 225, 235-242.  
7971971 A.Viel, and D.Branton (1994).
Interchain binding at the tail end of the Drosophila spectrin molecule.
  Proc Natl Acad Sci U S A, 91, 10839-10843.  
7706416 E.Fabbrizio, F.Pons, A.Robert, G.Hugon, A.Bonet-Kerrache, and D.Mornet (1994).
The dystrophin superfamily: variability and complexity.
  J Muscle Res Cell Motil, 15, 595-606.  
8034735 P.Matsudaira (1994).
The fimbrin and alpha-actinin footprint on actin.
  J Cell Biol, 126, 285-287.  
7656020 W.B.Gratzer (1994).
From helix to haemolysis.
  Nat Struct Biol, 1, 78-79.  
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 code is shown on the right.