1 Ocak 2021 Dergi makalesi Açık Erişim

Ciftci, Halilibrahim; Tateishi, Hiroshi; Koiwai, Kotaro; Koga, Ryoko; Anraku, Kensaku; Monde, Kazuaki; Dag, Cagdas; Destan, Ebru; Yuksel, Busra; Ayan, Esra; Yildirim, Gunseli; Yigin, Merve; Ertem, F. Betul; Shafiei, Alaleh; Guven, Omur; Besler, Sabri O.; Sierra, Raymond G.; Yoon, Chun Hong; Su, Zhen; Liang, Mengling; Liang, Mengling

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    "creators": [
      {
        "name": "Ciftci, Halilibrahim"
      }, 
      {
        "affiliation": "Kumamoto Univ, Fac Life Sci, Med & Biol Chem Sci Farm Joint Res Lab, Kumamoto 8620973, Japan", 
        "name": "Tateishi, Hiroshi"
      }, 
      {
        "affiliation": "KEK High Energy Accelerator Res Org, Inst Mat Struct Sci, Struct Biol Res Ctr, Tsukuba, Ibaraki 3050801, Japan", 
        "name": "Koiwai, Kotaro"
      }, 
      {
        "affiliation": "Kumamoto Univ, Fac Life Sci, Med & Biol Chem Sci Farm Joint Res Lab, Kumamoto 8620973, Japan", 
        "name": "Koga, Ryoko"
      }, 
      {
        "affiliation": "Kumamoto Hlth Sci Univ, Dept Med Technol, Kumamoto 8615598, Japan", 
        "name": "Anraku, Kensaku"
      }, 
      {
        "affiliation": "Kumamoto Univ, Fac Life Sci, Dept Microbiol, Kumamoto 8608556, Japan", 
        "name": "Monde, Kazuaki"
      }, 
      {
        "name": "Dag, Cagdas"
      }, 
      {
        "affiliation": "Stanford Pulse Inst, SLAC Natl Accelerator Lab, Menlo Pk, CA 94025 USA", 
        "name": "Destan, Ebru"
      }, 
      {
        "affiliation": "Stanford Pulse Inst, SLAC Natl Accelerator Lab, Menlo Pk, CA 94025 USA", 
        "name": "Yuksel, Busra"
      }, 
      {
        "affiliation": "Stanford Pulse Inst, SLAC Natl Accelerator Lab, Menlo Pk, CA 94025 USA", 
        "name": "Ayan, Esra"
      }, 
      {
        "affiliation": "Stanford Pulse Inst, SLAC Natl Accelerator Lab, Menlo Pk, CA 94025 USA", 
        "name": "Yildirim, Gunseli"
      }, 
      {
        "affiliation": "Stanford Pulse Inst, SLAC Natl Accelerator Lab, Menlo Pk, CA 94025 USA", 
        "name": "Yigin, Merve"
      }, 
      {
        "affiliation": "Koc Univ, Dept Mol Biol & Genet, TR-34450 Istanbul, Turkey", 
        "name": "Ertem, F. Betul"
      }, 
      {
        "affiliation": "Koc Univ, Dept Mol Biol & Genet, TR-34450 Istanbul, Turkey", 
        "name": "Shafiei, Alaleh"
      }, 
      {
        "affiliation": "Koc Univ, Dept Mol Biol & Genet, TR-34450 Istanbul, Turkey", 
        "name": "Guven, Omur"
      }, 
      {
        "affiliation": "Koc Univ, Dept Mol Biol & Genet, TR-34450 Istanbul, Turkey", 
        "name": "Besler, Sabri O."
      }, 
      {
        "affiliation": "SLAC Natl Accelerator Lab, Linac Coherent Light Source, Menlo Pk, CA USA", 
        "name": "Sierra, Raymond G."
      }, 
      {
        "affiliation": "SLAC Natl Accelerator Lab, Linac Coherent Light Source, Menlo Pk, CA USA", 
        "name": "Yoon, Chun Hong"
      }, 
      {
        "name": "Su, Zhen"
      }, 
      {
        "affiliation": "SLAC Natl Accelerator Lab, Linac Coherent Light Source, Menlo Pk, CA USA", 
        "name": "Liang, Mengling"
      }, 
      {
        "affiliation": "SLAC Natl Accelerator Lab, Linac Coherent Light Source, Menlo Pk, CA USA", 
        "name": "Liang, Mengling"
      }
    ], 
    "description": "Oligomerization of Pr55(Gag) is a critical step of the late stage of the HIV life cycle. It has been known that the binding of IP6, an abundant endogenous cyclitol molecule at the MA domain, has been linked to the oligomerization of Pr55(Gag). However, the exact binding site of IP6 on MA remains unknown and the structural details of this interaction are missing. Here, we present three high-resolution crystal structures of the MA domain in complex with IP6 molecules to reveal its binding mode. Additionally, extensive Differential Scanning Fluorimetry analysis combined with cryo- and ambient-temperature X-ray crystallography and GNM-based transfer entropy calculations identify the key residues that participate in IP6 binding. Our data provide novel insights about the multilayered HIV-1 virion assembly process that involves the interplay of IP6 with PIP2, a phosphoinositide essential for the binding of Pr55(Gag) to membrane. IP6 and PIP2 have neighboring alternate binding sites within the same highly basic region (residues 18-33). This indicates that IP6 and PIP2 bindings are not mutually exclusive and may play a key role in coordinating virion particles' membrane localization. Based on our three different IP6-MA complex crystal structures, we propose a new model that involves IP6 coordination of the oligomerization of outer MA and inner CA domain's 2D layers during assembly and budding.", 
    "doi": "10.1038/s41598-021-95236-8", 
    "has_grant": false, 
    "journal": {
      "issue": "1", 
      "title": "SCIENTIFIC REPORTS", 
      "volume": "11"
    }, 
    "license": {
      "id": "cc-by"
    }, 
    "publication_date": "2021-01-01", 
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    "resource_type": {
      "subtype": "article", 
      "title": "Dergi makalesi", 
      "type": "publication"
    }, 
    "science_branches": [
      "Di\u011fer"
    ], 
    "title": "Structural insight into host plasma membrane association and assembly of HIV-1 matrix protein"
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    1
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