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PDBsum entry 1qqf
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Immune system PDB id
1qqf

 

 

 

 

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Contents
Protein chain
277 a.a. *
Waters ×330
* Residue conservation analysis
PDB id:
1qqf
Name: Immune system
Title: N-terminally truncated c3d,g fragment of the complement system
Structure: Protein (complement c3dg). Chain: a. Fragment: n-terminally truncated fragment
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Tissue: plasma
Biol. unit: Dimer (from PDB file)
Resolution:
1.45Å     R-factor:   0.164     R-free:   0.217
Authors: G.Zanotti,A.Bassetto,R.Battistutta,M.Stoppini,R.Berni
Key ref: G.Zanotti et al. (2000). Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment. Biochim Biophys Acta, 1478, 232-238. PubMed id: 10825534 DOI: 10.1016/S0167-4838(00)00040-6
Date:
04-Jun-99     Release date:   31-Jul-00    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01026  (CO3_RAT) -  Complement C3 from Rattus norvegicus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1663 a.a.
277 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 

 
DOI no: 10.1016/S0167-4838(00)00040-6 Biochim Biophys Acta 1478:232-238 (2000)
PubMed id: 10825534  
 
 
Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment.
G.Zanotti, A.Bassetto, R.Battistutta, C.Folli, P.Arcidiaco, M.Stoppini, R.Berni.
 
  ABSTRACT  
 
Complement component C3 plays a key role in the complement-mediated immune defence, and occupies a central position within the complement cascade system. One of its degradation products, C3dg, was purified from rat serum and crystallised in two different crystal forms as N-terminally truncated fragment. Despite the truncation and the lack of a significant portion of the N-terminus as compared to C3d, the structure of the fragment is highly similar to that of recombinant human C3d (Nagar et al., Science 280 (1998) 1277-1281). Structural details of the reactive site have been obtained, suggesting a possible mode of thioester bond formation between Cys-1010 and Gln-1013 and thioester bond cleavage in the transacylation reaction involving His-1126. The truncation at the N-terminus of C3d leads to the exposure of a surface of the molecule that favours dimerisation, so that in both crystal forms, the fragment is present as a dimer, with monomers related by a two-fold axis.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19137065 Y.Ihm, W.O.Sparks, J.H.Lee, H.Cao, S.Carpenter, C.Z.Wang, K.M.Ho, and D.Dobbs (2009).
Structural model of the rev regulatory protein from equine infectious anemia virus.
  PLoS ONE, 4, e4178.  
17051152 A.Abdul Ajees, K.Gunasekaran, J.E.Volanakis, S.V.Narayana, G.J.Kotwal, and H.M.Murthy (2006).
The structure of complement C3b provides insights into complement activation and regulation.
  Nature, 444, 221-225.
PDB code: 2hr0
11264593 S.Sharma, T.Jabeen, R.K.Singh, R.Bredhorst, C.W.Vogel, C.Betzel, and T.P.Singh (2001).
Structural studies on the cobra venom factor: isolation, purification, crystallization and preliminary crystallographic analysis.
  Acta Crystallogr D Biol Crystallogr, 57, 596-598.  
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.

 

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