1qg5

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{{STRUCTURE_1qg5| PDB=1qg5 | SCENE= }}
{{STRUCTURE_1qg5| PDB=1qg5 | SCENE= }}
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'''HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORM A)'''
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===HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORM A)===
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==Overview==
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The crystal structures of beta-lactoglobulin genetic variants A and B have been determined in the orthorhombic space group C222(1) (lattice Y) by X-ray diffraction at 2.0 A and 1.95 A resolution, respectively. The structural comparison shows that both variants exhibit the open conformation of the EF loop at the pH of crystallization (pH 7.9), in contrast to what has been reported for the same genetic variants at pH 7.1 in the trigonal space group P3221 (lattice Z) [Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. &amp; Jameson, G.B. (1999) Protein Sci. 8, 75-83]. Furthermore, it was found that the stereochemical environment of Tyr42 changes significantly with pH variation between pH 7 and pH 8. This may provide a structural explanation for an as yet unexplained feature of the Tanford transition, namely the increase in exposure of a tyrosine residue.
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{{ABSTRACT_PUBMED_11168385}}
==About this Structure==
==About this Structure==
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[[Category: Isoform some]]
[[Category: Isoform some]]
[[Category: Lipocalin]]
[[Category: Lipocalin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:38:02 2008''

Revision as of 23:38, 28 July 2008

Template:STRUCTURE 1qg5

HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORM A)

Template:ABSTRACT PUBMED 11168385

About this Structure

1QG5 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition., Oliveira KM, Valente-Mesquita VL, Botelho MM, Sawyer L, Ferreira ST, Polikarpov I, Eur J Biochem. 2001 Jan;268(2):477-83. PMID:11168385

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