1bmg
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(New page: 200px<br /><applet load="1bmg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bmg, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 09:38, 20 November 2007
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CRYSTAL STRUCTURE OF BOVINE BETA2-MICROGLOBULIN
Overview
The three-dimensional structure of beta 2-microglobulin, the light chain, of the major histocompatibility complex class I antigens, has been, determined by x-ray crystallography. An electron density map of the bovine, protein was calculated at a nominal resolution of 2.9 A by using the, methods of multiple isomorphous replacement and electron density, modification refinement. The molecule is approximately 45 X 25 X 20 A in, size. Almost half of the amino acid residues participate in two large beta, structures, one of four strands and the other of three, linked by a, central disulfide bond. The molecule thus strongly resembles Ig constant, domains in polypeptide chain folding and overall tertiary structure. Amino, acid residues that are the same in the sequences of beta 2-microglobulin, and Ig constant domains are predominantly in the interior of the molecule, whereas residues conserved among beta 2-microglobulins from different, species are both in the interior and on the molecular surface. In the, crystals studied, the molecule is clearly monomeric, consistent with the, observation that beta 2-microglobulin, unlike Ig constant domains, apparently does not form dimers in vivo but associates with the heavy, chains of major histocompatibility complex antigens. Our results, demonstrate that, at the level of detailed three-dimensional structure, the light chain of the major histocompatibility class I antigens belongs, to a superfamily of structures related to the Ig constant domains.
About this Structure
1BMG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of beta 2-microglobulin., Becker JW, Reeke GN Jr, Proc Natl Acad Sci U S A. 1985 Jun;82(12):4225-9. PMID:3889925
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