DOI: 10.1073/pnas.91.18.8636. X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.

X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.

10.1073/pnas.91.18.8636

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.

Bibliography

Fedorov, A. A., Magnus, K. A., Graupe, M. H., Lattman, E. E., Pollard, T. D., & Almo, S. C. (1994). X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates. Proceedings of the National Academy of Sciences, 91(18), 8636â8640.

Authors 6

A A Fedorov (first)
K A Magnus (additional)
M H Graupe (additional)
E E Lattman (additional)
T D Pollard (additional)
S C Almo (additional)

References 0 Referenced 65

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 8:53 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 1:56 p.m.)
Indexed	2 months ago (June 26, 2025, 9:10 a.m.)
Issued	31 years ago (Aug. 30, 1994)
Published	31 years ago (Aug. 30, 1994)
Published Online	31 years ago (Aug. 30, 1994)
Published Print	31 years ago (Aug. 30, 1994)

Funders 0

None

BibTeX

@article{Fedorov_1994, title={X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.}, volume={91}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.91.18.8636}, DOI={10.1073/pnas.91.18.8636}, number={18}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Fedorov, A A and Magnus, K A and Graupe, M H and Lattman, E E and Pollard, T D and Almo, S C}, year={1994}, month=aug, pages={8636–8640} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        6,
        26
      ]
    ],
    "date-time": "2025-06-26T13:10:28Z",
    "timestamp": 1750943428111
  },
  "reference-count": 0,
  "publisher": "Proceedings of the National Academy of Sciences",
  "issue": "18",
  "content-domain": {
    "domain": [
      "www.pnas.org"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        1994,
        8,
        30
      ]
    ]
  },
  "abstract": "<jats:p>We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.</jats:p>",
  "DOI": "10.1073/pnas.91.18.8636",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2006,
        5,
        31
      ]
    ],
    "date-time": "2006-05-31T12:53:55Z",
    "timestamp": 1149080035000
  },
  "page": "8636-8640",
  "update-policy": "http://dx.doi.org/10.1073/pnas.cm10313",
  "source": "Crossref",
  "is-referenced-by-count": 65,
  "title": "X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.",
  "prefix": "10.1073",
  "volume": "91",
  "author": [
    {
      "given": "A A",
      "family": "Fedorov",
      "sequence": "first",
      "affiliation": [
        {
          "name": "Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461."
        }
      ]
    },
    {
      "given": "K A",
      "family": "Magnus",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461."
        }
      ]
    },
    {
      "given": "M H",
      "family": "Graupe",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461."
        }
      ]
    },
    {
      "given": "E E",
      "family": "Lattman",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461."
        }
      ]
    },
    {
      "given": "T D",
      "family": "Pollard",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461."
        }
      ]
    },
    {
      "given": "S C",
      "family": "Almo",
      "sequence": "additional",
      "affiliation": [
        {
          "name": "Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461."
        }
      ]
    }
  ],
  "member": "341",
  "published-online": {
    "date-parts": [
      [
        1994,
        8,
        30
      ]
    ]
  },
  "container-title": "Proceedings of the National Academy of Sciences",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://pnas.org/doi/pdf/10.1073/pnas.91.18.8636",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2022,
        4,
        13
      ]
    ],
    "date-time": "2022-04-13T17:56:26Z",
    "timestamp": 1649872586000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://pnas.org/doi/full/10.1073/pnas.91.18.8636"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1994,
        8,
        30
      ]
    ]
  },
  "references-count": 0,
  "journal-issue": {
    "issue": "18",
    "published-print": {
      "date-parts": [
        [
          1994,
          8,
          30
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1073/pnas.91.18.8636"
  ],
  "URL": "http://dx.doi.org/10.1073/pnas.91.18.8636",
  "relation": {},
  "ISSN": [
    "0027-8424",
    "1091-6490"
  ],
  "subject": [],
  "container-title-short": "Proc. Natl. Acad. Sci. U.S.A.",
  "published": {
    "date-parts": [
      [
        1994,
        8,
        30
      ]
    ]
  },
  "assertion": [
    {
      "value": "1994-08-30",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}