1bk2
From Proteopedia
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| - | [[Image:1bk2.jpg|left|200px]] | + | [[Image:1bk2.jpg|left|200px]] |
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| - | '''A-SPECTRIN SH3 DOMAIN D48G MUTANT''' | + | {{Structure |
| + | |PDB= 1bk2 |SIZE=350|CAPTION= <scene name='initialview01'>1bk2</scene>, resolution 2.01Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''A-SPECTRIN SH3 DOMAIN D48G MUTANT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BK2 is a [ | + | 1BK2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BK2 OCA]. |
==Reference== | ==Reference== | ||
| - | Obligatory steps in protein folding and the conformational diversity of the transition state., Martinez JC, Pisabarro MT, Serrano L, Nat Struct Biol. 1998 Aug;5(8):721-9. PMID:[http:// | + | Obligatory steps in protein folding and the conformational diversity of the transition state., Martinez JC, Pisabarro MT, Serrano L, Nat Struct Biol. 1998 Aug;5(8):721-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9699637 9699637] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sh3-domain]] | [[Category: sh3-domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:06 2008'' |
Revision as of 08:12, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
A-SPECTRIN SH3 DOMAIN D48G MUTANT
Overview
We have analyzed the existence of obligatory steps in the folding reaction of the alpha-spectrin SH3 domain by mutating Asp 48 (D48G), which is at position i+3 of an isolated two-residue type II' beta-turn. Calorimetry and X-ray analysis show an entropic stabilizing effect resulting from local changes at the dihedral angles of the beta-turn. Kinetic analysis of D48G shows that this beta-turn is fully formed in the transition state, while there is no evidence of its formation in an isolated fragment. Introduction of several mutations in the D48G protein reveals that the local stabilization has not significantly altered the transition state ensemble. All these results, together with previous analysis of other alpha-spectrin and src SH3 mutants, indicate that: (i) in the folding reaction there could be obligatory steps which are not necessarily part of the folding nucleus; (ii) transition state ensembles in beta-sheet proteins could be quite defined and conformationally restricted ('mechanic folding nucleus'); and (iii) transition state ensembles in some proteins could be evolutionarily conserved.
About this Structure
1BK2 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Obligatory steps in protein folding and the conformational diversity of the transition state., Martinez JC, Pisabarro MT, Serrano L, Nat Struct Biol. 1998 Aug;5(8):721-9. PMID:9699637
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