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1cj5

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|ACTIVITY=
|ACTIVITY=
|GENE= BLG CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
|GENE= BLG CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cj5 OCA], [http://www.ebi.ac.uk/pdbsum/1cj5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cj5 RCSB]</span>
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[[Category: dynamic]]
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Revision as of 16:22, 30 March 2008


PDB ID 1cj5

Drag the structure with the mouse to rotate
Gene: BLG CDNA (Bos taurus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



BOVINE BETA-LACTOGLOBULIN A


Overview

Using heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine beta-lactoglobulin A at pH 2.0 and 45 degrees C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight-stranded continuous antiparallel beta-barrel and one major alpha-helix, is similar to the X-ray dimeric structure obtained at pH 6.2, including betaI-strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. [1H]-15N NOE revealed that betaF, betaG, and betaH strands buried under the major alpha-helix are rigid on a pico- to nanosecond time scale and also emphasized rapid fluctuations of loops and the N- and C-terminal regions.

About this Structure

1CJ5 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Solution structure and dynamics of bovine beta-lactoglobulin A., Kuwata K, Hoshino M, Forge V, Era S, Batt CA, Goto Y, Protein Sci. 1999 Nov;8(11):2541-5. PMID:10595563

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