Annotations for this protein have been verified by the authors of the corresponding papers



DP00270: Fab DNA-1FASTA viewXML view

General information
DisProt:DP00270
Name:Fab DNA-1
Synonym(s):Antigen binding fragment DNA-1
anti-ssDNA Fab DNA-1
First appeared in release:Release 3.0 (02/17/2006)
UniProt: 
UniGene:Mm.342177
SwissProt:  
TrEMBL:  
NCBI (GI): 3399661
Source organism:Mus musculus (Mouse)
Sequence length:220
Percent disordered:5%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
LESGPELVKP GASVKMSCKA SGYTFTSYVM HWVKQKPGQG LEWIGYINPY NDGTKYNEKF - 60
KGKATLTSDK SSSTAYMELS SLTSEDSAVY YCVRGGYRPY YAMDYWGQGT SVTVSSAKTT - 120
PPSVYPLAPG SAAQTNSMVT LGCLVKGYFP EPVTVTWNSG SLSSGVHTFP AVLQSDLYTL - 180
SSSVTVPSST WPSETVTCNV AHPASSTKVD KKIVPRDCTS

Region 1: 97-100 Region 2: 95-105

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:apical residues of HCDR3
Location:97 - 100
Length:4
Region sequence:

YRPY

Modification type:  
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Protein-DNA binding
Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (298 K; isopranol 20 %; PEG4000 (w/v) 14 %; sodium citrate (pH 5.5) 0.1 M)

References:
  1. Schuermann JP, Prewitt SP, Davies C, Deutscher SL, Tanner JJ. "Evidence for structural plasticity of heavy chain complementarity-determining region 3 in antibody-ssDNA recognition." J Mol Biol. 2005; 347(5): 965-78. PubMed: 15784256

Comments:
 



Region 2
Type:Disordered
Name:HCDR3
Location:95 - 105
Length:11
Region sequence:

GGYRPYYAMDY

Modification type:  
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (isopropanol 20 %; PEG4000 (w/v) 14 %; sodium citrate (pH 5.5) 0.1 M)

References:
  1. Calcutt MJ, Kremer MT, Giblin MF, Quinn TP, Deutscher SL. "Isolation and characterization of nucleic acid-binding antibody fragments from autoimmune mice-derived bacteriophage display libraries." Gene. 1993; 137(1): 77-83. PubMed: 7506692

  2. Schuermann JP, Prewitt SP, Davies C, Deutscher SL, Tanner JJ. "Evidence for structural plasticity of heavy chain complementarity-determining region 3 in antibody-ssDNA recognition." J Mol Biol. 2005; 347(5): 965-78. PubMed: 15784256

Comments:
 



References

  1. Calcutt MJ, Kremer MT, Giblin MF, Quinn TP, Deutscher SL. "Isolation and characterization of nucleic acid-binding antibody fragments from autoimmune mice-derived bacteriophage display libraries." Gene. 1993; 137(1): 77-83. PubMed: 7506692



Comments


A UniProt ID cannot be located for this protein. The Vh sequence for DNA-1 is similar to an anti-ssDNA mAB from NZB x NZW F1 autoimmune mice (NCBI Accession CAA80108.1, GI 297744). In UniProt, there is 98% sequence identity with entries P01868 and P01869, the IgG-1 chain C region.


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