.
The Open Protein Structure Annotation Network
PDB Keyword
.

1r73

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title NMR for structural proteomics of Thermotoga maritima: Screening and structure determination. J.STRUCT.FUNCT.GENOM. 5 205-215 2004
    Site JCSG
    PDB Id 1r73 Target Id 283349
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1293,TM1492 Molecular Weight 7972.04 Da.
    Residues 66 Isoelectric Point 10.27
    Sequence mkaselrnytdeelknlleekkrqlmelrfqlamgqlkntslikltkrdiariktilrerelgirr
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The gene TM1492 from Thermotoga maritima encodes 50S ribosomal protein L29 PF00831 COG0255, a superfamily of ribosomal L29 protein/HIP proteins.  As expected, theses proteins are well-conserved among different bacteria species.  L29 is a protein of the large ribosomal subunit. A homolog, called heparin/heparan sulfate interacting protein (HIP), has also been identified in mammals. L29 is located on the surface of the large ribosomal subunit, where it participates in forming a protein ring that surrounds the polypeptide exit channel, providing structural support for the ribosome. L29 is involved in forming the translocon binding site, along with L19, L22, L23, L24, and L31e. In addition, L29 and L23 form the interaction site for trigger factor (TF) on the ribosomal surface, adjacent to the exit tunnel. L29 forms numerous interactions with L23 and with the 23S rRNA. In some eukaryotes, L29 is referred to as L35, which is distinct from L35 found in bacteria and some eukaryotes (primarily plastids and mitochondria). The mammalian homolog, HIP, is found on the surface of many tissues and cell lines. It is believed to play a role in cell adhesion and modulation of blood coagulation [Ref]. It has also been shown to inhibit apoptosis in cancer cells [Ref].  Interestingly, in human lungs and small intestines, HIP acts as a major broad-spectrum antimicrobial protein [Ref].

    Ligand Summary



    References

    Reviews

    References

     

    1. Wang J and Rabenstein DL Interaction of heparin with two synthetic peptides that neutralize the anticoagulant activity of heparin. Biochemistry. 2006 Dec 26; 45(51):15740-7 PubMed HubMed doi:10.1021/bi061346a pmid:17176096.

       


      Discuss this publication
    2. Liu JJ, Zhang J, Ramanan S, Julian J, Carson DD, and Hooi SC Heparin/heparan sulfate interacting protein plays a role in apoptosis induced by anticancer drugs. Carcinogenesis. 2004 Jun; 25(6):873-9 PubMed HubMed doi:10.1093/carcin/bgh081 pmid:14729579.

       


      Discuss this publication
    3. Meyer-Hoffert U, Hornef M, Henriques-Normark B, Normark S, Andersson M, and P眉tsep K Identification of heparin/heparan sulfate interacting protein as a major broad-spectrum antimicrobial protein in lung and small intestine. FASEB J. 2008 Jul; 22(7):2427-34 PubMed HubMed doi:10.1096/fj.07-103440 pmid:18299334.

       


      Discuss this publication
    Tag page

    Files (0)

     
    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch