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Regulating PAS domain function with foreign PAS ligands

a technology domain functions, applied in the field of foreign pas ligands of protein regulatory domains, can solve problems such as evidence of such cofactors, and achieve the effect of convenient detection

Inactive Publication Date: 2006-03-09
BOARD OF RGT THE UNIV OF TEXAS SYST
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0015] The PAS domain may be isolated or expressed by and within a host cell or animal, wherein the ligand is foreign to the host, and the change is

Problems solved by technology

However, for most PAS domains there is no evidence for such a cofactor.

Method used

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  • Regulating PAS domain function with foreign PAS ligands
  • Regulating PAS domain function with foreign PAS ligands
  • Regulating PAS domain function with foreign PAS ligands

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Embodiment Construction

[0021] In one aspect of the invention, we show that foreign ligands can be introduced into the hydrophobic core regions of PAS domains even (a) where the PAS domain does not require a core-bound ligand for formation or function; (b) the PAS domain is fully folded in its native state; c) where there is no NMR-apparent a priori formed core cavity to accommodate such a ligand; and / or (d) wherein the PAS domain is unassociated with any predetermined ligand-dependent heterologous chaperone protein. In contrast, AHR PAS-B binds both HSP90, a common chaperone of unfolded proteins, and ligand, and the AHR PAS-B domain is unfolded without ligand (e.g. Kikuchi, et al., 2003, J Biochem 134, 83-90).

[0022] This aspect of the invention provides methods and corresponding compositions, kits, instructions and business methods for detecting binding of a PAS domain with a foreign (i.e. not a natural ligand of the PAS domain) core ligand of the PAS domain, wherein the PAS domain is predetermined, pref...

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Abstract

A functional surface binding specificity of a PAS domain, wherein the PAS domain is predetermined, prefolded in its native state, and comprises a hydrophobic core that has no NMR-apparent a priori formed ligand cavity, is changed by (a) introducing into the hydrophobic core of the PAS domain a foreign ligand of the PAS domain; and (b) detecting a change in the functional surface binding specificity of the PAS domain.

Description

CROSS REFERENCE TO RELATED APPLICATIONS [0001] This application is a continuation of Ser. No. 10 / 677,734, and a continuation-in-part of Ser. No.10 / 059,962, which is a division of Ser. No. 09 / 770,170, now U.S. Pat No. 6,319,679.GOVERNMENT RIGHTS [0002] This work was supported by National Institute of Health Grants CA90601 and CA95471. The U.S. government may have rights in any patent issuing on this application.INTRODUCTION [0003] 1. Field of the Invention [0004] The field of this invention is foreign ligands of PAS protein regulatory domains. [0005] 2. Background of the Invention [0006] PAS (Per-ARNT-Sim) domains are protein interaction domains widely used for intra- and intermolecular associations. Database searches indicate that the PAS domain family contains over 3000 members distributed in all kingdoms of life. Structural studies reveal a common mixed a / b fold predicted to be present in all members of this family (Crews & Fan, 1999; Pellequer et al., 1998). [0007] Some members o...

Claims

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Application Information

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IPC IPC(8): C12Q1/48C12N9/12
CPCC12N9/12C12Q1/485G01N2500/20G01N2500/00G01N33/573
Inventor GARDNER, KEVIN H.AMEZCUA, CARLOS A.ERBEL, PAULUS J.A.CARD, PAUL B.HARPER, SHANNONRUTTER, JAREDBRUICK, RICHARDMCKNIGHT, STEVEN L.
Owner BOARD OF RGT THE UNIV OF TEXAS SYST