Literature DB >> 11106166

The PA domain: a protease-associated domain.

P Mahon1, A Bateman.   

Abstract

We have identified a similarity between the apical domain of the human transferrin receptor and several other protein families. This domain is found associated with two different families of peptidases. Therefore, we term it the PA domain for protease-associated domain. The PA domain is found inserted within a loop of the peptidase domain of family M8/M33 zinc peptidases. The PA domain is also found in a vacuolar sorting receptor and a ring finger protein of unknown function that may be a cell surface receptor. The PA domain may mediate substrate determination of peptidases or form protein-protein interactions.

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Year:  2000        PMID: 11106166      PMCID: PMC2144460          DOI: 10.1110/ps.9.10.1930

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  18 in total

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Authors:  N Paris; S W Rogers; L Jiang; T Kirsch; L Beevers; T E Phillips; J C Rogers
Journal:  Plant Physiol       Date:  1997-09       Impact factor: 8.340

5.  Interaction of a potential vacuolar targeting receptor with amino- and carboxyl-terminal targeting determinants.

Authors:  T Kirsch; G Saalbach; N V Raikhel; L Beevers
Journal:  Plant Physiol       Date:  1996-06       Impact factor: 8.340

6.  Characterization and glutamyl preferring carboxypeptidase function of prostate specific membrane antigen: a novel folate hydrolase.

Authors:  W D Heston
Journal:  Urology       Date:  1997-03       Impact factor: 2.649

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8.  Alternatively spliced variants of prostate-specific membrane antigen RNA: ratio of expression as a potential measurement of progression.

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  28 in total

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6.  Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase.

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8.  The single subunit transmembrane E3 ligase gene related to anergy in lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins across the cell membrane.

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9.  Cutting edge: The transmembrane E3 ligase GRAIL ubiquitinates the costimulatory molecule CD40 ligand during the induction of T cell anergy.

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10.  Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3.

Authors:  Christian Ottmann; Rolf Rose; Franziska Huttenlocher; Anna Cedzich; Patrick Hauske; Markus Kaiser; Robert Huber; Andreas Schaller
Journal:  Proc Natl Acad Sci U S A       Date:  2009-09-23       Impact factor: 11.205

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