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3A98

Crystal structure of the complex of the interacting regions of DOCK2 and ELMO1

Summary for 3A98
Entry DOI10.2210/pdb3a98/pdb
DescriptorDedicator of cytokinesis protein 2, Engulfment and cell motility protein 1 (3 entities in total)
Functional Keywordsprotein-protein complex, dock2, elmo1, sh3 domain, ph domain, helix bundle, proline-rich sequence, cytoskeleton, guanine-nucleotide releasing factor, membrane, phosphoprotein, apoptosis, cell membrane, phagocytosis, sh3-binding, signaling protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight89621.78
Authors
Hanawa-Suetsugu, K.,Kukimoto-Niino, M.,Sekine, S.,Ito, T.,Mishima-Tsumagari, C.,Terada, T.,Shirouzu, M.,Fukui, Y.,Yokoyama, S. (deposition date: 2009-10-21, release date: 2010-10-27, Last modification date: 2019-09-04)
Primary citationHanawa-Suetsugu, K.,Kukimoto-Niino, M.,Mishima-Tsumagari, C.,Akasaka, R.,Ohsawa, N.,Sekine, S.,Ito, T.,Tochio, N.,Koshiba, S.,Kigawa, T.,Terada, T.,Shirouzu, M.,Nishikimi, A.,Uruno, T.,Katakai, T.,Kinashi, T.,Kohda, D.,Fukui, Y.,Yokoyama, S.
Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms.
Proc.Natl.Acad.Sci.USA, 109:3305-3310, 2012
Cited by
PubMed: 22331897
DOI: 10.1073/pnas.1113512109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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