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Angiogenic tyrosyl trna synthetase compositions and methods

An angiogenesis and enzyme synthesis technology, applied in the field of angiogenic TyrRS protein variants and its angiogenic fragments to stimulate angiogenesis, can solve the problem of no cytokine activity

Active Publication Date: 2008-12-31
THE SCRIPPS RES INST
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  • Abstract
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  • Claims
  • Application Information

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Problems solved by technology

In each case, the full-length enzyme has synthetase function but no cytokine activity

Method used

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  • Angiogenic tyrosyl trna synthetase compositions and methods
  • Angiogenic tyrosyl trna synthetase compositions and methods
  • Angiogenic tyrosyl trna synthetase compositions and methods

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Embodiment Construction

[0026] DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENT

[0027] Amino acid residues in proteins have been classified in different ways, mainly based on the physicochemical characteristics conferred by the amino acid side chains. For example, one general classification includes three classes of amino acids: (1) hydrophobic (nonpolar) amino acids, including glycine, alanine, valine, phenylalanine, proline, methionine, isoleucine, amino acids; (2) charged amino acids, including aspartic acid, glutamic acid, lysine, and arginine; and (3) polar amino acids, including serine, threonine, tyrosine, Histidine, cysteine, asparagine, glutamine, and tryptophan; glycine is sometimes included in the fourth class, by itself (see Chapter 1 of Branden and Tooze, Introduction to Protein Structure, Second Edition, Garland Publishing, Inc. 1998, pages 3-12, which are incorporated herein by reference).

[0028] Amino acid residues can be further classified according to whether their side chains...

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Abstract

The present invention provides an isolated tyrosyl tRNA synthetase (TyrRS) polypeptide variant which comprises (a) a Rossmann fold region or a portion thereof, preferably including an alpha5 coil; and (b) an anticodon recognition domain or portion thereof, preferably including an alpha14 coil. Preferably, the alpha5 coil and the alpha14 coil have a greater spatial separation in the tertiary structure of the variant compared to the corresponding spatial separation in native human TyrRS. The variant preferably comprises an amino acid residue sequence identity of at least about 50 % compared to the amino acid residue sequence of human TyrRS (SEQ ID NO: 3), includes at least one non-conservative amino acid residue substitution relative to the amino acid residue sequence of human TyrRS, and preferably presents an exposed ELR motif in the alpha5 coil on an external portion of the tertiary structure of the polypeptide. A preferred TyrRS protein variant comprises the amino acid residue sequence of SEQ ID NO: 4 or a portion thereof. The proteins and protein fragments of the invention are angiogenic and are useful for stimulating angiogenesis in mammalian tissues.

Description

[0001] Cross-references to related applications [0002] This application claims the benefit of US Provisional Application Serial No. 60 / 741,580, filed December 2, 2005, which is incorporated herein by reference. [0003] Statement of Government Interest [0004] Part of the work described here was funded by National Institutes of Health grant number CA92577. The US Government has certain rights in this invention. field of invention [0005] The present invention relates to angiogenic tyrosyl tRNA synthetase (TyrRS) compositions. More particularly the present invention relates to angiogenic TyrRS protein variants and angiogenic fragments thereof, and methods of stimulating angiogenesis thereby. Background of the invention [0006] Aminoacyl-tRNA synthetases are essential enzymes that catalyze the loading of amino acids onto cognate tRNAs as the first step in protein synthesis. These essential enzymes are classified into two types based on the presence of unique sequen...

Claims

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Application Information

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IPC IPC(8): C12Q1/68C12N5/07C12N5/071C12N5/077
CPCC12N9/93A61P17/02A61P19/02A61P29/00A61P43/00A61P9/00
Inventor X·-L·杨
Owner THE SCRIPPS RES INST
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