1dyn

<table><tr><td colspan='2'>[[1dyn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DYN FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dyn OCA], [https://pdbe.org/1dyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dyn RCSB], [https://www.ebi.ac.uk/pdbsum/1dyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dyn ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/DYN1_HUMAN 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.

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== 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<ref>PMID:7954789</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Ferguson, K M]]

[[Category: Lemmon, M A]]

[[Category: Schlessinger, J]]

[[Category: Sigler, P B]]

[[Category: Signal transduction protein]]