1mcp

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PHOSPHOCHOLINE BINDING IMMUNOGLOBULIN FAB MC/PC603. AN X-RAY DIFFRACTION STUDY AT 2.7 ANGSTROMS

Structural highlights

1mcp is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HVM20_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the Fab of McPC603, a phosphocholine-binding mouse myeloma protein, has been refined at 2.7 A resolution by a combination of restrained least-squares refinement and molecular modeling. The overall structure remains as previously reported, with an elbow bend angle between the variable and constant modules of 133 degrees. Some adjustments have been made in the structure of the loops as a result of the refinement. The hypervariable loops are all visible in the electron density map with the exception of three residues in the first hypervariable loop of the light chain. A sulfate ion occupies the site of binding of the phosphate moiety of phosphocholine.

Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A.,Satow Y, Cohen GH, Padlan EA, Davies DR J Mol Biol. 1986 Aug 20;190(4):593-604. PMID:3097327[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
45 reviews cite this structure
Conformations of immunoglobulin hypervariable regions.
Chothia et al. (1989)
44 more
268 other articles
No citations found

See Also

References

  1. ↑ Satow Y, Cohen GH, Padlan EA, Davies DR. Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A. J Mol Biol. 1986 Aug 20;190(4):593-604. PMID:3097327

Contents


PDB ID 1mcp

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OCA

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