2mcg: Difference between revisions
New page: left|200px<br /> <applet load="2mcg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mcg, resolution 2.0Å" /> '''THREE-DIMENSIONAL ST... |
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'''THREE-DIMENSIONAL STRUCTURE OF A LIGHT CHAIN DIMER CRYSTALLIZED IN WATER. CONFORMATIONAL FLEXIBILITY OF A MOLECULE IN TWO CRYSTAL FORMS'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF A LIGHT CHAIN DIMER CRYSTALLIZED IN WATER. CONFORMATIONAL FLEXIBILITY OF A MOLECULE IN TWO CRYSTAL FORMS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2MCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 1MCG. Full crystallographic information is available from [http:// | 2MCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 1MCG. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MCG OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:37:52 2008'' | ||
Revision as of 18:37, 15 February 2008
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THREE-DIMENSIONAL STRUCTURE OF A LIGHT CHAIN DIMER CRYSTALLIZED IN WATER. CONFORMATIONAL FLEXIBILITY OF A MOLECULE IN TWO CRYSTAL FORMS
OverviewOverview
The three-dimensional structure of an immunoglobulin light chain dimer, (Mcg) crystallized in deionized water (orthorhombic form) was determined, at 2.0 A resolution by phase extension and crystallographic refinement., This structure was refined side-by-side with that of the same molecule, crystallized in ammonium sulfate (trigonal form). The dimer adopted, markedly different structures in the two solvents. "Elbow bend" angles, between pseudo 2-fold axes of rotation relating pairs of "variable" (V), and "constant" (C) domains were found to be 132 degrees in the, orthorhombic form and 115 degrees in the trigonal form. Modes of, association of the V domains and, to a lesser extent, the pairing, interactions of the C domains were different in the two structures., Alterations in the V domain pairing were reflected in the shapes of the, binding regions and in the orientations of the side-chains lining the, walls of the binding sites. In the trigonal form, for instance, the V, domain interface was compartmentalized into a main binding cavity and a, deep pocket, whereas these spaces were continuous in the orthorhombic, structure. Patterns of ordered water molecules were quite distinct in the, two crystal types. In some cases, the solvent structures could be, correlated with conformational changes in the proteins. For example, close, contacts between V and C domains of monomer 1 of the trigonal form were, not retained in orthorhombic crystals. Ordered water molecules filled the, space created when the two domains moved apart.
About this StructureAbout this Structure
2MCG is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 1MCG. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms., Ely KR, Herron JN, Harker M, Edmundson AB, J Mol Biol. 1989 Dec 5;210(3):601-15. PMID:2515285
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