2dyn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:19, 14 February 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)==
==DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)==
-
<StructureSection load='2dyn' size='340' side='right' caption='[[2dyn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+
<StructureSection load='2dyn' size='340' side='right'caption='[[2dyn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2dyn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DYN FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2dyn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DYN FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dyn OCA], [http://pdbe.org/2dyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dyn RCSB], [http://www.ebi.ac.uk/pdbsum/2dyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dyn ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=2dyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dyn OCA], [https://pdbe.org/2dyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dyn RCSB], [https://www.ebi.ac.uk/pdbsum/2dyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dyn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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.
+
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dyn ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dyn ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
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.
 
- 
-
Crystal structure of the pleckstrin homology domain from dynamin.,Timm D, Salim K, Gout I, Guruprasad L, Waterfield M, Blundell T Nat Struct Biol. 1994 Nov;1(11):782-8. PMID:7634088<ref>PMID:7634088</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 2dyn" style="background-color:#fffaf0;"></div>
 
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
-
[[Category: Timm, D E]]
+
[[Category: Large Structures]]
-
[[Category: Motor protein]]
+
[[Category: Timm DE]]
-
[[Category: Phospholipid binding]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Signal transduction]]
+

Current revision

DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)

PDB ID 2dyn

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools