GREMLIN Database
PF07452 - CHRD proteinLast updated: 1465465832

Organism: META    
Function: known
Type: SOL
Uniprot: G4QGG7
Pfam: PF07452. CHRD. 7 hits. 
Co-evolution data: G4QGG7

TMalign/SCOP results:
  • 0.64 d2jlpa_ (Immunoglobulin-like beta-sandwich)
  • 0.62 d1xtma_ (Immunoglobulin-like beta-sandwich)
  • 0.62 d1pzsa_ (Immunoglobulin-like beta-sandwich)
  • 0.61 d2wyta_ (Immunoglobulin-like beta-sandwich)
  • 0.60 d2axoa1 (Thioredoxin fold)
Trends Biochem Sci. 2003 Sep;28(9):470-3.
CHRD, a novel domain in the BMP inhibitor chordin, is also found in microbial proteins.

CHRD (after SWISSPROT abbreviation for chordin) is a novel domain identified in chordin, an inhibitor of bone morphogenetic proteins. Database searches have revealed several microbial homologues to this domain. It is anticipated to have an immunoglobulin-like beta-barrel structure based on limited similarity to superoxide dismutases but, as yet, no clear functional prediction can be made
1. Chordin contains four novel repeats

2. Conserved features of the CHRD domains: The most conserved feature of the CHRD domain is the C-terminal GE[I/L]RGQ[V/I/L] motif. No single residue is fully conserved between all the domains, but several highly conserved positions can be found between the microbial CHRD domains. Many of these residues are also present in the third repeat of chordin, which raises the possibility that the other domains in chordin have lost the original function and gained a new, perhaps structural or regulatory, role.

Four cysteine residues are fully conserved in the inter-vWC sequences between the chordin orthologues, which would be predicted to form disulfide bonds in an extracellular protein such as chordin. Two of these map outside the canonical CHRD domains immediately after the second and fourth domains (not shown in the alignment). The two other fully conserved cysteine residues are not in equivalent positions, and are found within the first and fourth domains. This would suggest that disulfide bonds connecting these residues are formed between the domains and would, thus, define the orientation of the domains with respect to each other.


http://www.sciencedirect.com/science/article/pii/S0968000403001713

Models
Name DB Rc Date Action
Model G4QGG7_UNI 1.013 12May2016 View - Download
Model G4QGG7_UNI 1.013 12May2016 View - Download
Model G4QGG7_UNI 1.013 12May2016 View - Download
Model G4QGG7_UNI 1.010 12May2016 View - Download
Model G4QGG7_UNI 1.009 12May2016 View - Download
Model - REFINE G4QGG7_UNI 0.947 12Jun2016 View - Download
Files
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G4QGG7_models.png

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