STRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAINSTRUCTURE OF M2BP SCAVENGER RECEPTOR CYSTEINE-RICH DOMAIN

Structural highlights

1by2 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, RCSB, PDBsum

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

Scavenger receptor cysteine-rich (SRCR) domains are found widely in cell surface molecules and in some secreted proteins, where they are thought to mediate ligand binding. We have determined the crystal structure at 2.0 A resolution of the SRCR domain of Mac-2 binding protein (M2BP), a tumor-associated antigen and matrix protein. The structure reveals a curved six-stranded beta-sheet cradling an alpha-helix. Structure-based sequence alignment demonstrates that the M2BP SRCR domain is a valid template for the entire SRCR protein superfamily. This allows an interpretation of previous mutagenesis data on ligand binding to the lymphocyte receptor CD6.

Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily.,Hohenester E, Sasaki T, Timpl R Nat Struct Biol. 1999 Mar;6(3):228-32. PMID:10074941[1]

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

References

  1. Hohenester E, Sasaki T, Timpl R. Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily. Nat Struct Biol. 1999 Mar;6(3):228-32. PMID:10074941 doi:http://dx.doi.org/10.1038/6669

1by2, resolution 2.00Å

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