PDBsum entry 2b1u

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protein links
Metal binding protein PDB id
Jmol PyMol
Protein chain
71 a.a. *
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Solution structure of calmodulin-like skin protein c terminal domain
Structure: Calmodulin-like protein 5. Chain: a. Fragment: c terminal domain. Synonym: calmodulin-like skin protein. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: calml5. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: E.Babini,I.Bertini,F.Capozzi,E.Chirivino,C.Luchinat, Structural Proteomics In Europe (Spine)
Key ref:
E.Babini et al. (2006). A structural and dynamic characterization of the EF-hand protein CLSP. Structure, 14, 1029-1038. PubMed id: 16765896 DOI: 10.1016/j.str.2006.04.004
16-Sep-05     Release date:   30-May-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9NZT1  (CALL5_HUMAN) -  Calmodulin-like protein 5
146 a.a.
71 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  


DOI no: 10.1016/j.str.2006.04.004 Structure 14:1029-1038 (2006)
PubMed id: 16765896  
A structural and dynamic characterization of the EF-hand protein CLSP.
E.Babini, I.Bertini, F.Capozzi, E.Chirivino, C.Luchinat.
The structure and dynamics of human calmodulin-like skin protein (CLSP) have been characterized by NMR spectroscopy. The mobility of CLSP has been found to be different for the N-terminal and C-terminal domains. The isolated domains were also expressed and analyzed. The structure of the isolated C-terminal domain is presented. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain. By exploiting the capability of Tb3+ bound to CLSP to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. By using NMR, ITC, and ESI-MS, the calcium and magnesium binding properties were investigated. Finally, CLSP is framed into the evolutionary scheme of the calmodulin-like family.
  Selected figure(s)  
Figure 3.
Figure 3. Relaxation Parameters
^15N relaxation parameters of full-length CLSP measured at 500 MHz and 25°C.
Figure 4.
Figure 4. Comparison of CaM Structure and CLSP Model
Space-filling representation of the experimental CaM N-terminal domain structure (PDB:1CFC) and of the CLSP N-terminal domain model. The model was generated by the program MODELLER (6v2) with the N-terminal domain of CaM (PDB: 1CFC) as template. (A), (B), and (C) refer to different orientations of the protein structures.
  The above figures are reprinted by permission from Cell Press: Structure (2006, 14, 1029-1038) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21312310 W.Ohashi, H.Hirota, and T.Yamazaki (2011).
Solution structure and fluctuation of the Mg(2+)-bound form of calmodulin C-terminal domain.
  Protein Sci, 20, 690-701.
PDB code: 2rrt
19592703 X.Huang, M.Beullens, J.Zhang, Y.Zhou, E.Nicolaescu, B.Lesage, Q.Hu, J.Wu, M.Bollen, and Y.Shi (2009).
Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21).
  J Biol Chem, 284, 25375-25387.
PDB code: 2jxw
19722697 Y.Liu, and J.A.Cowan (2009).
Iron-sulfur cluster biosynthesis: characterization of a molten globule domain in human NFU.
  Biochemistry, 48, 7512-7518.  
18280495 E.Johnson, L.Bruschweiler-Li, S.A.Showalter, G.W.Vuister, F.Zhang, and R.Brüschweiler (2008).
Structure and dynamics of Ca2+-binding domain 1 of the Na+/Ca2+ exchanger in the presence and in the absence of Ca2+.
  J Mol Biol, 377, 945-955.  
18200608 O.Okhrimenko, and I.Jelesarov (2008).
A survey of the year 2006 literature on applications of isothermal titration calorimetry.
  J Mol Recognit, 21, 1.  
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.