spacer
spacer

PDBsum entry 1aey
Go to PDB code: 
protein links
Cytoskeleton PDB id
1aey

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
58 a.a. *
* Residue conservation analysis
PDB id:
1aey
Name: Cytoskeleton
Title: Alpha-spectrin src homology 3 domain, solution nmr, 15 structures
Structure: Alpha-spectrin. Chain: a. Fragment: src homology 3 domain. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: brain. Cellular_location: cytoskeleton. Expressed in: escherichia coli. Expression_system_taxid: 469008.
NMR struc: 15 models
Authors: F.J.Blanco,A.R.Ortiz,L.Serrano
Key ref: F.J.Blanco et al. (1997). 1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure. J Biomol Nmr, 9, 347-357. PubMed id: 9255941
Date:
02-Mar-97     Release date:   15-May-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P07751  (SPTN1_CHICK) -  Spectrin alpha chain, non-erythrocytic 1 from Gallus gallus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		2477 a.a.
58 a.a.
Key:    Secondary structure  CATH domain

 

 
J Biomol Nmr 9:347-357 (1997)
PubMed id: 9255941  
 
 
1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure.
F.J.Blanco, A.R.Ortiz, L.Serrano.
 
  ABSTRACT  
 
The assignment of the 1H and 15N nuclear magnetic resonance spectra of the Src-homology region 3 domain of chicken brain alpha-spectrin has been obtained. A set of solution structures has been determined from distance and dihedral angle restraints, which provide a reasonable representation of the protein structure in solution, as evaluated by a principal component analysis of the global pairwise root-mean-square deviation (rmsd) in a large set of structures consisting of the refined and unrefined solution structures and the crystal structure. The solution structure is well defined, with a lower degree of convergence between the structures in the loop regions than in the secondary structure elements. The average pairwise rmsd between the 15 refined solution structures is 0.71 +/- 0.13 A for the backbone atoms and 1.43 +/- 0.14 A for all heavy atoms. The solution structure is basically the same as the crystal structure. The average rmsd between the 15 refined solution structures and the crystal structure is 0.76 A for the backbone atoms and 1.45 +/- 0.09 A for all heavy atoms. There are, however, small differences probably caused by intermolecular contacts in the crystal structure.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19582374 J.Xu, Y.Xue, and N.R.Skrynnikov (2009).
Detection of nanosecond time scale side-chain jumps in a protein dissolved in water/glycerol solvent.
  J Biomol NMR, 45, 57-72.  
17407569 S.Casares, E.Ab, H.Eshuis, O.Lopez-Mayorga, N.A.van Nuland, and F.Conejero-Lara (2007).
The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3.
  BMC Struct Biol, 7, 22.
PDB codes: 2jm8 2jm9 2jma
12945054 H.Fan, and A.E.Mark (2003).
Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
  Proteins, 53, 111-120.  
12496075 E.Paci, M.Vendruscolo, and M.Karplus (2002).
Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.
  Biophys J, 83, 3032-3038.  
11948879 B.J.van Rossum, F.Castellani, K.Rehbein, J.Pauli, and H.Oschkinat (2001).
Assignment of the nonexchanging protons of the alpha-spectrin SH3 domain by two- and three-dimensional 1H-13C solid-state magic-angle spinning NMR and comparison of solution and solid-state proton chemical shifts.
  Chembiochem, 2, 906-914.  
  11206053 M.C.Vega, J.C.Martínez, and L.Serrano (2000).
Thermodynamic and structural characterization of Asn and Ala residues in the disallowed II' region of the Ramachandran plot.
  Protein Sci, 9, 2322-2328.
PDB codes: 1qkw 1qkx
9888794 J.C.Martínez, A.R.Viguera, R.Berisio, M.Wilmanns, P.L.Mateo, V.V.Filimonov, and L.Serrano (1999).
Thermodynamic analysis of alpha-spectrin SH3 and two of its circular permutants with different loop lengths: discerning the reasons for rapid folding in proteins.
  Biochemistry, 38, 549-559.
PDB code: 1pwt
10413463 M.Sadqi, S.Casares, M.A.Abril, O.López-Mayorga, F.Conejero-Lara, and E.Freire (1999).
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
  Biochemistry, 38, 8899-8906.  
9565752 E.Lacroix, A.R.Viguera, and L.Serrano (1998).
Reading protein sequences backwards.
  Fold Des, 3, 79-85.  
9699637 J.C.Martinez, M.T.Pisabarro, and L.Serrano (1998).
Obligatory steps in protein folding and the conformational diversity of the transition state.
  Nat Struct Biol, 5, 721-729.
PDB code: 1bk2
9485402 K.W.Plaxco, J.I.Guijarro, C.J.Morton, M.Pitkeathly, I.D.Campbell, and C.M.Dobson (1998).
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
  Biochemistry, 37, 2529-2537.  
9566119 D.C.Dalgarno, M.C.Botfield, and R.J.Rickles (1997).
SH3 domains and drug design: ligands, structure, and biological function.
  Biopolymers, 43, 383-400.  
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.

 

spacer
spacer