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Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns.

Abstract：

:The experiments described here explore the role of local sequence in the folding of cellular retinoic acid binding protein I (CRABP I). This is a 136-residue, 10-stranded, antiparallel beta-barrel protein with seven beta-hairpins and is a member of the intracellular lipid binding protein (iLBP) family. The relative roles of local and global sequence information in governing the folding of this class of proteins are not well-understood. In question is whether the beta-turns are locally defined by short-range interactions within their sequences, and are thus able to play an active role in reducing the conformational space available to the folding chain, or whether the turns are passive, relying upon global forces to form. Short (six- and seven-residue) peptides corresponding to the seven CRABP I turns were analyzed by circular dichroism and NMR for their tendencies to take up the conformations they adopt in the context of the native protein. The results indicate that two of the peptides, encompassing turns III and IV in CRABP I, have a strong intrinsic bias to form native turns. Intriguingly, these turns are on linked hairpins in CRABP I and represent the best-conserved turns in the iLBP family. These results suggest that local sequence may play an important role in narrowing the conformational ensemble of CRABP I during folding.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Rotondi KS,Gierasch LM

doi

10.1021/bi034304k

subject

Has Abstract

pub_date

2003-07-08 00:00:00

pages

7976-85

issue

26

eissn

0006-2960

issn

1520-4995

journal_volume

42

pub_type

杂志文章

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