2DYN

DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)

Summary for 2DYN

• Entry DOI: 10.2210/pdb2dyn/pdb
• Descriptor: DYNAMIN (2 entities in total)
• Functional Keywords: motor protein, phospholipid binding, protein binding, signal transduction
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q05193
• Total number of polymer chains: 2
• Total formula weight: 28860.78

Authors

Timm, D.E. (deposition date: 1997-07-21, release date: 1997-11-12, Last modification date: 2024-02-14)

Primary citation

Timm, D.,Salim, K.,Gout, I.,Guruprasad, L.,Waterfield, M.,Blundell, T.
Crystal structure of the pleckstrin homology domain from dynamin.
Nat.Struct.Biol., 1:782-788, 1994

PubMed Abstract: The pleckstrin homology (PH) domain is a conserved module present in many signal transducing and cytoskeletal proteins. Here we report the 2.8 A crystal structure of the PH domain from dynamin. This domain consists of seven beta-strands forming two roughly orthogonal antiparallel beta-sheets terminating with an amphipathic alpha-helix. The structure also reveals a non-covalent dimeric association of the PH domain and a hydrophobic pocket surrounded by a charged rim. The dynamin PH domain structure is discussed in relation to its potential role in mediating interactions between proteins.

PubMed: 7634088
DOI: 10.1038/nsb1194-782

Experimental method

X-RAY DIFFRACTION (2.3 Å)