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PDBsum entry 3ncm

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protein links
Cell adhesion protein PDB id
3ncm
Jmol
Contents
Protein chain
92 a.a. *
* Residue conservation analysis
PDB id:
3ncm
Name: Cell adhesion protein
Title: Neural cell adhesion molecule, module 2, nmr, 20 structures
Structure: Protein (neural cell adhesion molecule, large isoform). Chain: a. Fragment: module 2. Synonym: ncam module 2. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Strain: escherichia coli strain top 10 f'. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
NMR struc: 20 models
Authors: P.H.Jensen,V.Soroka,N.K.Thomsen,V.Berezin,E.Bock,F.M.Poulsen
Key ref:
P.H.Jensen et al. (1999). Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion. Nat Struct Biol, 6, 486-493. PubMed id: 10331878 DOI: 10.1038/8292
Date:
21-Sep-98     Release date:   23-Jul-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13595  (NCAM1_MOUSE) -  Neural cell adhesion molecule 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1115 a.a.
92 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1038/8292 Nat Struct Biol 6:486-493 (1999)
PubMed id: 10331878  
 
 
Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion.
P.H.Jensen, V.Soroka, N.K.Thomsen, I.Ralets, V.Berezin, E.Bock, F.M.Poulsen.
 
  ABSTRACT  
 
The structure in solution of the second Ig-module fragment of residues 117-208 of NCAM has been determined. Like the first Ig-module of residues 20-116, it belongs to the I set of the immunogloblin superfamily. Module 1 and module 2 interact weakly, and the binding sites of this interaction have been identified. The two-module fragment NCAM(20-208) is a stable dimer. Removal of the charged residues in these sites in NCAM(20-208) abolishes the dimerization. Modeling the dimer of NCAM(20-208) to fit the interactions of these charges produces one coherent binding site for the formation of two antiparallel strands of the first two NCAM modules. This mode of binding could be a major element in trans-cellular interactions in neural cell adhesion.
 
  Selected figure(s)  
 
Figure 6.
Figure 6. Model building of the dimer of NCAM(20−208) in a MOLMOL ribbon presentation. The two monomers of the dimer are labeled a and b, with 1a indicating the location of module 1 in monomer a, and so on. Strands are shown in blue and helical turns in red.
Figure 7.
Figure 7. The dimer of NCAM(20−208). a, Ribbon presentation of the dimer, with designations as in Fig. 6. Monomers a and b are colored gray and magenta, respectively. Cyan marks the binding−site residues in module 1 as in Fig. 2b; yellow marks the corresponding residues in module 2 as in Fig. 2e. b, Space-filling model of the two-module dimer of NCAM(20−208). The residues of the binding sites in the two modules are colored as in (a). In addition, the residues used for modeling the dimer are shown in dark-blue on module 1 and in green on module 2. Residues Phe 38 and Phe 201 that are complementary in the dimer and potential sites of hydrophobic interactions are also labeled. c, Closeup of the six salt bridges and the two hydrophobic interactions used to model the dimer of the first two modules of NCAM(20−208).
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1999, 6, 486-493) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19383447 V.Maruthamuthu, K.Schulten, and D.Leckband (2009).
Elasticity and rupture of a multi-domain neural cell adhesion molecule complex.
  Biophys J, 96, 3005-3014.  
18593816 A.Kochoyan, F.M.Poulsen, V.Berezin, E.Bock, and V.V.Kiselyov (2008).
Structural basis for the activation of FGFR by NCAM.
  Protein Sci, 17, 1698-1705.  
19305742 D.Kiryushko, E.Bock, and V.Berezin (2007).
Pharmacology of cell adhesion molecules of the nervous system.
  Curr Neuropharmacol, 5, 253-267.  
16197499 G.G.Skibo, I.V.Lushnikova, K.Y.Voronin, O.Dmitrieva, T.Novikova, B.Klementiev, E.Vaudano, V.A.Berezin, and E.Bock (2005).
A synthetic NCAM-derived peptide, FGL, protects hippocampal neurons from ischemic insult both in vitro and in vivo.
  Eur J Neurosci, 22, 1589-1596.  
16188877 J.A.Wieland, A.A.Gewirth, and D.E.Leckband (2005).
Single molecule adhesion measurements reveal two homophilic neural cell adhesion molecule bonds with mechanically distinct properties.
  J Biol Chem, 280, 41037-41046.  
16181411 N.Kulahin, O.Rudenko, V.Kiselyov, F.M.Poulsen, V.Berezin, and E.Bock (2005).
Modulation of the homophilic interaction between the first and second Ig modules of neural cell adhesion molecule by heparin.
  J Neurochem, 95, 46-55.  
16045455 V.V.Kiselyov, V.Soroka, V.Berezin, and E.Bock (2005).
Structural biology of NCAM homophilic binding and activation of FGFR.
  J Neurochem, 94, 1169-1179.  
15118102 C.P.Johnson, I.Fujimoto, C.Perrin-Tricaud, U.Rutishauser, and D.Leckband (2004).
Mechanism of homophilic adhesion by the neural cell adhesion molecule: use of multiple domains and flexibility.
  Proc Natl Acad Sci U S A, 101, 6963-6968.  
15465311 D.Leckband (2004).
Nanomechanics of adhesion proteins.
  Curr Opin Struct Biol, 14, 524-530.  
12770907 B.Zhu, S.Chappuis-Flament, E.Wong, I.E.Jensen, B.M.Gumbiner, and D.Leckband (2003).
Functional analysis of the structural basis of homophilic cadherin adhesion.
  Biophys J, 84, 4033-4042.  
12431225 L.C.Rønn, M.Olsen, V.Soroka, S.ØStergaard, S.Dissing, F.M.Poulsen, A.Holm, V.Berezin, and E.Bock (2002).
Characterization of a novel NCAM ligand with a stimulatory effect on neurite outgrowth identified by screening a combinatorial peptide library.
  Eur J Neurosci, 16, 1720-1730.  
11983682 V.Soroka, D.Kiryushko, V.Novitskaya, L.C.Ronn, F.M.Poulsen, A.Holm, E.Bock, and V.Berezin (2002).
Induction of neuronal differentiation by a peptide corresponding to the homophilic binding site of the second Ig module of the neural cell adhesion molecule.
  J Biol Chem, 277, 24676-24683.  
11514671 A.E.Kister, M.A.Roytberg, C.Chothia, J.M.Vasiliev, and I.M.Gelfand (2001).
The sequence determinants of cadherin molecules.
  Protein Sci, 10, 1801-1810.  
10820224 A.G.Foley, B.P.Hartz, H.C.Gallagher, L.C.Rønn, V.Berezin, E.Bock, and C.M.Regan (2000).
A synthetic peptide ligand of neural cell adhesion molecule (NCAM) IgI domain prevents NCAM internalization and disrupts passive avoidance learning.
  J Neurochem, 74, 2607-2613.  
11087873 B.Kachar, M.Parakkal, M.Kurc, Y.Zhao, and P.G.Gillespie (2000).
High-resolution structure of hair-cell tip links.
  Proc Natl Acad Sci U S A, 97, 13336-13341.  
10842356 K.L.Crossin, and L.A.Krushel (2000).
Cellular signaling by neural cell adhesion molecules of the immunoglobulin superfamily.
  Dev Dyn, 218, 260-279.  
10899941 L.C.Rønn, P.Doherty, A.Holm, V.Berezin, and E.Bock (2000).
Neurite outgrowth induced by a synthetic peptide ligand of neural cell adhesion molecule requires fibroblast growth factor receptor activation.
  J Neurochem, 75, 665-671.  
10753817 M.C.Deller, and E.Yvonne Jones (2000).
Cell surface receptors.
  Curr Opin Struct Biol, 10, 213-219.  
10757969 S.Y.Lee, and R.E.Klevit (2000).
The whole is not the simple sum of its parts in calmodulin from S. cerevisiae.
  Biochemistry, 39, 4225-4230.  
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.