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Journal article
Structure of the SH3 domain of rat endophilin A2
Acta crystallographica. Section F, Structural biology communications, v 64(4), pp 243-246
01 Apr 2008
PMID: 18391417
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Abstract
The crystal structure of the SH3 domain of rat endophilin A2 has been determined by the multiwavelength anomalous dispersion method and refined at a resolution of 1.70 angstrom to R and R-free values of 0.196 and 0.217, respectively. The structure adheres to the canonical SH3-domain fold and is highly similar to those of the corresponding domains of endophilins A1 and A3. An intermolecular packing interaction between two molecules in the lattice exploits features that are commonly observed in SH3-domain ligand recognition, including the insertion of a proline side chain into the ligand-binding groove of the protein and the recognition of a basic residue by a cluster of acidic side chains on the RT loop.
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Details
- Title
- Structure of the SH3 domain of rat endophilin A2
- Creators
- Patrick J. Loll - Drexel UniversityEvelyn Swain - Drexel UniversityYuan Chen - Department of Molecular Physiology and Biophysics, Jefferson Medical College, 1020 Locust Street, Philadelphia, PA 19107, USABrian T. Turner - Drexel UniversityJi-fang Zhang - Department of Molecular Physiology and Biophysics, Jefferson Medical College, 1020 Locust Street, Philadelphia, PA 19107, USA
- Publication Details
- Acta crystallographica. Section F, Structural biology communications, v 64(4), pp 243-246
- Publisher
- Int Union Crystallography
- Number of pages
- 4
- Grant note
- R01-MH73060; R01 MH073060 / NIMH NIH HHS; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of Mental Health (NIMH) R01MH073060 / NATIONAL INSTITUTE OF MENTAL HEALTH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of Mental Health (NIMH)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000254473200004
- Scopus ID
- 2-s2.0-41949099163
- Other Identifier
- 991019170552404721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemical Research Methods
- Biochemistry & Molecular Biology
- Biophysics
- Crystallography