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PDBsum entry 2per

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protein ligands links
Electron transport PDB id
2per

 

 

 

 

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Contents
Protein chain
222 a.a. *
Ligands
MNB
Waters ×68
* Residue conservation analysis
PDB id:
2per
Name: Electron transport
Title: Crystal structure of human chloride intracellular channel protein 2
Structure: Chloride intracellular channel protein 2. Chain: a. Synonym: xap121. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: liver. Gene: clic2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.00Å     R-factor:   0.218     R-free:   0.258
Authors: X.D.Su,Y.H.Liang,W.Mi
Key ref:
W.Mi et al. (2008). The crystal structure of human chloride intracellular channel protein 2: a disulfide bond with functional implications. Proteins, 71, 509-513. PubMed id: 18186468 DOI: 10.1002/prot.21922
Date:
03-Apr-07     Release date:   04-Mar-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O15247  (CLIC2_HUMAN) -  Chloride intracellular channel protein 2 from Homo sapiens
Seq:
Struc:
247 a.a.
222 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.1.11.1.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: E.C.1.8.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
DOI no: 10.1002/prot.21922 Proteins 71:509-513 (2008)
PubMed id: 18186468  
 
 
The crystal structure of human chloride intracellular channel protein 2: a disulfide bond with functional implications.
W.Mi, Y.H.Liang, L.Li, X.D.Su.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Structure of human CLIC2. (A) Structure based sequence alignment of human CLIC1-6 and DHAR2, DHAR3 from A. thaliana. Identical and conserved residues are colored in red and yellow, respectively. CXXC motif is colored in cyan and marked by upwards triangles. The additional N-terminal sequences of CLIC5 and CLIC6 were truncated. (B) Overall structure of CLIC2. N-terminal domain is colored in red; C-terminal domain in green, the joint loop in yellow, the foot loop in blue, disulfide bond between Cys^30 and Cys^33 is showed as stick (yellow). (C) Structure superimposition of CLIC1 (yellow), CLIC4 (red) structures on CLIC2 (green). Disulfide bond in CLIC2 is showed in stick (yellow).
Figure 2.
Figure 2. Disulfide bond between Cys^30 and Cys^33 and the electrostatic potential surface of CLIC2. (A) Structure comparison between the N-terminal domain of CLIC2 (green) and pig glutaredoxin (magenta), poxviral glutaredoxin (cyan). The disulfide bond of CLIC2 is showed in stick (yellow). (B) 2Fo-Fc electron density map and stick diagram of the disulfide bond in human CLIC2. (C) Structure comparison of disulfide bonds between CLIC2 (green) with pig glutaredoxin (magenta), poxviral glutaredoxin (cyan). (D) The electrostatic potential surface of CLIC2 and foot loop insertion into the cavity of the neighbor molecule.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 71, 509-513) copyright 2008.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20934451 D.W.Song, J.G.Lee, H.S.Youn, S.H.Eom, and d.o. .H.Kim (2011).
Ryanodine receptor assembly: a novel systems biology approach to 3D mapping.
  Prog Biophys Mol Biol, 105, 145-161.  
19650640 S.H.Stoychev, C.Nathaniel, S.Fanucchi, M.Brock, S.Li, K.Asmus, V.L.Woods, and H.W.Dirr (2009).
Structural dynamics of soluble chloride intracellular channel protein CLIC1 examined by amide hydrogen-deuterium exchange mass spectrometry.
  Biochemistry, 48, 8413-8421.  
19356589 X.Meng, G.Wang, C.Viero, Q.Wang, W.Mi, X.D.Su, T.Wagenknecht, A.J.Williams, Z.Liu, and C.C.Yin (2009).
CLIC2-RyR1 interaction and structural characterization by cryo-electron microscopy.
  J Mol Biol, 387, 320-334.  
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.

 

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