title: High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.
abstract: The alpha-spectrin SH3 domain (Spc-SH3) is a small modular domain which has been broadly used as a model protein in folding studies and these studies have sometimes been supported by structural information obtained from the coordinates of Spc-SH3 mutants. The structure of B5/D48G, a multiple mutant designed to improve the hydrophobic core and as a consequence the protein stability, has been solved at 1 A resolution. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=24.79, b=37.23, c=62.95 A. This mutant also bears a D48G substitution in the distal loop and this mutation has also been reported to increase the stability of the protein by itself. The structure of the B5/D48G mutant shows a highly packed hydrophobic core and a more ordered distal loop compared with previous Spc-SH3 structures.
authors.affiliation: Departamento de Química-Física, Bioquímica y Química Inorgánica, Universidad de Almería, Carretera Sacramento, Almería 04120, Spain. acamara@ual.es
authors.forename: Ana
authors.initials: A
authors.lastname: Cámara-Artigas
authors.forename: Monserrat
authors.initials: M
authors.lastname: Andújar-Sánchez
authors.forename: Emilia
authors.initials: E
authors.lastname: Ortiz-Salmerón
authors.forename: Celia
authors.initials: C
authors.lastname: Cuadri
authors.forename: Eva S
authors.initials: ES
authors.lastname: Cobos
authors.forename: Jose Manuel
authors.initials: JM
authors.lastname: Martin-Garcia
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D009154:Mutation; D016415:Sequence Alignment; D013049:Spectrin / Q000737:chemistry* / Q000235:genetics; D018909:src Homology Domains
chemical_list: D013049:Spectrin
references.citation: Nat Struct Biol. 2002 Jun;9(6):485-93
references.pmid: 12006985
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):72-82
references.pmid: 16369096
references.citation: BMC Struct Biol. 2007 Apr 02;7:22
references.pmid: 17407569
references.citation: Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):337-40
references.pmid: 11173498
references.citation: Nat Struct Biol. 1998 Aug;5(8):721-9
references.pmid: 9699637
references.citation: Methods Mol Biol. 2008;426:419-35
references.pmid: 18542881
references.citation: Biochemistry. 1994 Mar 1;33(8):2142-50
references.pmid: 7509635
references.citation: Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1247-52
references.pmid: 19966410
references.citation: J Mol Biol. 2003 Apr 18;328(1):221-33
references.pmid: 12684010
references.citation: Nature. 1992 Oct 29;359(6398):851-5
references.pmid: 1279434
references.citation: Anal Biochem. 1989 Nov 1;182(2):319-26
references.pmid: 2610349
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21
references.pmid: 20057044
references.citation: Protein Sci. 2000 Dec;9(12):2322-8
references.pmid: 11206053
references.citation: Nat Struct Biol. 1999 Nov;6(11):1010-6
references.pmid: 10542091
references.citation: J Mol Biol. 2006 Feb 17;356(2):453-68
references.pmid: 16375922
references.citation: J Mol Biol. 2007 Sep 21;372(3):774-97
references.pmid: 17681537
references.citation: Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2834-9
references.pmid: 14978284
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):48-57
references.pmid: 16369093
references.citation: Proteins. 2007 May 15;67(3):531-47
references.pmid: 17330285
references.citation: Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
references.pmid: 15572765