KH domain

One motif, two folds

Research output: Contribution to journalArticle

171 Citations (Scopus)

Abstract

The K homology (KH) module is a widespread RNA-binding motif that has been detected by sequence similarity searches in such proteins as heterogeneous nuclear ribonucleoprotein K (hnRNP K) and ribosomal protein S3. Analysis of spatial structures of KH domains in hnRNP K and S3 reveals that they are topologically dissimilar and thus belong to different protein folds. Thus KH motif proteins provide a rare example of protein domains that share significant sequence similarity in the motif regions but possess globally distinct structures. The two distinct topologies might have arisen from an ancestral KH motif protein by N- and C-terminal extensions, or one of the existing topologies may have evolved from the other by extension, displacement and deletion. C-terminal extension (deletion) requires β-sheet rearrangement through the insertion (removal) of a β-strand in a manner similar to that observed in serine protease inhibitors serpins. Current analysis offers a new look on how proteins can change fold in the course of evolution.

Original languageEnglish (US)
Pages (from-to)638-643
Number of pages6
JournalNucleic Acids Research
Volume29
Issue number3
StatePublished - Feb 1 2001

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Heterogeneous-Nuclear Ribonucleoprotein K
Serpins
Amino Acid Motifs
Proteins
Spatial Analysis
Serine Proteinase Inhibitors
Protein C

ASJC Scopus subject areas

  • Genetics

Cite this

KH domain : One motif, two folds. / Grishin, N. V.

In: Nucleic Acids Research, Vol. 29, No. 3, 01.02.2001, p. 638-643.

Research output: Contribution to journalArticle

Grishin, N. V. / KH domain : One motif, two folds. In: Nucleic Acids Research. 2001 ; Vol. 29, No. 3. pp. 638-643.
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