3c98

<table><tr><td colspan='2'>[[3c98]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dn1 1dn1]. The November 2013 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''SNARE Proteins'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2013_11 10.2210/rcsb_pdb/mom_2013_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C98 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3C98 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dn1|1dn1]]</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=3c98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c98 OCA], [http://pdbe.org/3c98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c98 RCSB], [http://www.ebi.ac.uk/pdbsum/3c98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c98 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/STXB1_RAT STXB1_RAT]] May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions. [[http://www.uniprot.org/uniprot/STX1A_RAT STX1A_RAT]] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.

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== Publication Abstract from PubMed ==

Sec1/Munc18-like (SM) proteins functionally interact with SNARE proteins in vesicular fusion. Despite their high sequence conservation, structurally disparate binding modes for SM proteins with syntaxins have been observed. Several SM proteins appear to bind only to a short peptide present at the N terminus of syntaxin, designated the N-peptide, while Munc18a binds to a 'closed' conformation formed by the remaining portion of syntaxin 1a. Here, we show that the syntaxin 16 N-peptide binds to the SM protein Vps45, but the remainder of syntaxin 16 strongly enhances the affinity of the interaction. Likewise, the N-peptide of syntaxin 1a serves as a second binding site in the Munc18a/syntaxin 1a complex. When the syntaxin 1a N-peptide is bound to Munc18a, SNARE complex formation is blocked. Removal of the N-peptide enables binding of syntaxin 1a to its partner SNARE SNAP-25, while still bound to Munc18a. This suggests that Munc18a controls the accessibility of syntaxin 1a to its partners, a role that might be common to all SM proteins.

Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide.,Burkhardt P, Hattendorf DA, Weis WI, Fasshauer D EMBO J. 2008 Apr 9;27(7):923-33. Epub 2008 Mar 13. PMID:18337752<ref>PMID:18337752</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: Burkhardt, P]]

[[Category: Fasshauer, D]]

[[Category: Hattendorf, D A]]

[[Category: Misura, K M]]

[[Category: Scheller, R H]]

[[Category: Weis, W I]]

[[Category: Transport]]