1px2

<table><tr><td colspan='2'>[[1px2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PX2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PX2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pk8|1pk8]], [[1aux|1aux]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1px2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px2 OCA], [http://pdbe.org/1px2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1px2 RCSB], [http://www.ebi.ac.uk/pdbsum/1px2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1px2 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SYN1_RAT SYN1_RAT]] Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release.

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== Publication Abstract from PubMed ==

Synapsins are multidomain proteins that are critical for regulating neurotransmitter release in vertebrates. In the present study, two crystal structures of the C domain of rat synapsin I (rSynI-C) in complex with Ca(2+) and ATP reveal that this protein can form a tetramer and that a flexible loop (the "multifunctional loop") contacts bound ATP. Further experiments were carried out on a protein comprising the A, B, and C domains of rat synapsin I (rSynI-ABC). An ATP-stabilized tetramer of rSynI-ABC is observed during velocity sedimentation and size-exclusion chromatographic experiments. These hydrodynamic results also indicate that the A and B domains exist in an extended conformation. Calorimetric measurements of ATP binding to wild-type and mutant rSynI-ABC demonstrate that the multifunctional loop and a cross-tetramer contact are important for ATP binding. The evidence supports a view of synapsin I as an ATP-utilizing, tetrameric protein made up of monomers that have a flexible, extended N terminus.

Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I.,Brautigam CA, Chelliah Y, Deisenhofer J J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:14688264<ref>PMID:14688264</ref>

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

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== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Brautigam, C A]]

[[Category: Chelliah, Y]]

[[Category: Deisenhofer, J]]

[[Category: Atp binding]]

[[Category: Membrane protein]]