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PMID: 2987935 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Three-dimensional structure of ubiquitin at 2.8 A resolution.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 82 ·No. 11 ·1985-06-00 ·Pages 3582-5

Vijay-Kumar S, Bugg CE, Wilkinson KD, Cook WJ

Abstract

The three-dimensional structure of ubiquitin has been determined at 2.8 A resolution. X-ray diffraction data for the native protein and derivatives were collected with an automated diffractometer. Phases were obtained by use of a single isomorphous mercuric acetate derivative. The molecule contains a pronounced hydrophobic core. Prominent secondary structural features include three and one-half turns of alpha-helix, a mixed beta-sheet that contains four strands, and seven reverse turns. The histidine, tyrosine, and two phenylalanine residues are located on the surface of the molecule.

MeSH Terms
Amino Acid Sequence High Mobility Group Proteins Humans Macromolecular Substances Mathematics Models, Molecular Ubiquitins X-Ray Diffraction
Chemicals
High Mobility Group Proteins Macromolecular Substances Ubiquitins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Vijay-Kumar S
Bugg C E
Wilkinson K D
Cook W J
References (27)
27 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.82.11.3582
Published
1985-06-00
Pages
3582-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC397829
Subset
IM
Grants
NCI NIH HHS · CA-13148 · United States
NIDCR NIH HHS · DE-02670 · United States
NIGMS NIH HHS · GM-27144 · United States
External Links
PubMed source DOI: 10.1073/pnas.82.11.3582 PMC Full Text View journal details
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