Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency

被引：51

作者：

Carey, Jannette ^{[1
]}

Lindman, Stina

Bauer, Mikael

Linse, Sara

机构：

[1] Princeton Univ, Dept Chem, Princeton, NJ 08544 USA

[2] Lund Univ, Ctr Chem, Dept Biophys Chem, S-22100 Lund, Sweden

来源：

PROTEIN SCIENCE | 2007年 / 16卷 / 11期

关键词：

stability; metastability; steric constraints; cooperativity; ligand binding;

D O I：

10.1110/ps.072985007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The phenomena of protein reconstitution and three-dimensional domain swapping reveal that highly similar structures can be obtained whether a protein is comprised of one or more polypeptide chains. In this review, we use protein reconstitution as a lens through which to examine the range of protein tolerance to chain interruptions and the roles of the primary structure in related features of protein structure and folding, including circular permutation, natively unfolded proteins, allostery, and amyloid fibril formation. The results imply that noncovalent interactions in a protein are sufficient to specify its structure under the constraints imposed by the covalent backbone.

引用

页码：2317 / 2333

页数：17

共 118 条

[1]

Amzel LM, 1997, PROTEINS, V28, P144

[2]

ANDRIA G, 1971, J BIOL CHEM, V246, P7421

[3] The domain-swapped dimer of cyanovirin-N is in a metastable folded state: Reconciliation of X-ray and NMR structures [J].