3NGP

High resolution structure of alpha-spectrin SH3 domain mutant with a redesigned core

Summary for 3NGP

• Entry DOI: 10.2210/pdb3ngp/pdb
• Related: 1shg
• Descriptor: Spectrin alpha chain, brain (2 entities in total)
• Functional Keywords: beta barrel, structural protein
• Biological source: Gallus gallus (bantam,chickens)
• Cellular location: Cytoplasm, cytoskeleton: P07751
• Total number of polymer chains: 1
• Total formula weight: 7209.28

Authors

Camara-Artigas, A.,Gavira, J.A.,Martin-Garcia, J.M. (deposition date: 2010-06-12, release date: 2010-09-08, Last modification date: 2023-09-06)

Primary citation

Camara-Artigas, A.,Andujar-Sanchez, M.,Ortiz-Salmeron, E.,Cuadri, C.,Cobos, E.S.,Martin-Garcia, J.M.
High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.
Acta Crystallogr.,Sect.F, 66:1023-1027, 2010

PubMed 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.

PubMed: 20823517
DOI: 10.1107/S1744309110030095

Experimental method

X-RAY DIFFRACTION (1.084 Å)