Structural highlights
Function
[DYN1_HUMAN] Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray crystal structure of the pleckstrin homology (PH) domain from human dynamin has been refined to 2.2 A resolution. A seven-stranded beta sandwich of two orthogonal antiparallel beta sheets is closed at one corner by a C-terminal alpha helix. Opposite this helix are the three loops that vary most among PH domains. The basic fold is very similar to that of two other PH domains recently determined by nuclear magnetic resonance, confirming that PH domain with known structure is electrostatically polarized, with the three variable loops forming a positively charged surface. This surface includes the position of the X-linked immunodeficiency mutation in the Btk PH domain and may serve as a ligand-binding surface.
Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin.,Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB Cell. 1994 Oct 21;79(2):199-209. PMID:7954789[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. Cell. 1994 Oct 21;79(2):199-209. PMID:7954789
