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Review
. 2005:80:349-74.
doi: 10.1016/S0079-6603(05)80009-1.

Ribonuclease inhibitor: structure and function

Kimberly A Dickson  1 , Marcia C Haigis, Ronald T Raines
Affiliations
Review

Ribonuclease inhibitor: structure and function

Kimberly A Dickson et al. Prog Nucleic Acid Res Mol Biol. 2005.
No abstract available

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Figures

Fig. 1
Fig. 1
Three-dimensional structures of RI and its complexes with ribonucleases. (A) Porcine RI (6) with colors corresponding to exon-encoded modules (40). (B) Porcine RI·RNase A complex (51) (C) Human RI·ANG complex (69).
Fig. 2
Fig. 2
Alignment of the amino acid sequences of RI from human (8), porcine (7), mouse (40), and rat (39). The consensus sequence for the A-type and B-type repeats is indicated, along with the corresponding secondary structure. The initiator methionine residue was not detected in the N-terminal tryptic fragment of human RI and is shown in parentheses. Conserved residues are in boxes. Residues of human RI that contact ANG (69) and residues of porcine RI that contact RNase A (51) are shaded.
Fig. 3
Fig. 3
(A) Typical A-type of RI (residues 138–165). Typical B-type repeat of RI (residues 223–252). The side chains of conserved aliphatic residues are shown explicitly and numbered within the repeat.
Fig. 4
Fig. 4
Structures of five representative LRR proteins (Table III). (A) cysteine-containing protein Skp2 (57). (B) Plant-specific protein Pgip (58). (C) SDS22-Like protein U2A′ (55). (D) Bacterial protein YopM (56). (E) Decorin (59).
See this image and copyright information in PMC

References

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    1. Lee FS, Vallee BL. Structure and action of mammalian ribonuclease (angiogenin) inhibitor. Progress Nucl Acid Res Molec Biol. 1993;44:1–30. - PubMed
    1. Hofsteenge J. Ribonuclease inhibitor. In: D’Alessio G, Riordan JF, editors. Ribonucleases: Structures and Functions. Academic Press; New York: 1997. pp. 621–658.
    1. Shapiro R. Cytoplasmic ribonuclease inhibitor. Methods Enzymol. 2001;341:611–628. - PubMed

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