Literature DB >> 3384017

Nucleotide binding to the rod outer segment rim protein.

T A Shuster1, A K Nagy, D B Farber.   

Abstract

The rod photoreceptor outer segment maintains a remarkable morphology. Two of the proteins which have been implicated in the maintenance of this structure are the 240 kDa spectrin-like protein, and the 220 kDa glycoprotein often referred to as the rim protein. We have probed rat rod outer segment proteins with light-activated (azido-labeled) radioactive nucleotides and found a nucleotide binding site(s) on the rim protein which has a preference for guanine nucleotides. Binding to this site is stimulated by the divalent cations zinc, manganese and magnesium, but not calcium. This site is under investigation and may play a role in stabilizing protein structure.

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Year:  1988        PMID: 3384017     DOI: 10.1016/s0014-4835(88)80053-8

Source DB:  PubMed          Journal:  Exp Eye Res        ISSN: 0014-4835            Impact factor:   3.467


  1 in total

1.  Direct zinc binding to purified rhodopsin and disc membranes.

Authors:  T A Shuster; A K Nagy; D C Conly; D B Farber
Journal:  Biochem J       Date:  1992-02-15       Impact factor: 3.857

  1 in total

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