|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5a9h' size='340' side='right'caption='[[5a9h]], [[Resolution|resolution]] 2.06Å' scene=''> | | <StructureSection load='5a9h' size='340' side='right'caption='[[5a9h]], [[Resolution|resolution]] 2.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a9h]] is a 1 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=5A9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A9H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a9d|5a9d]], [[5a9i|5a9i]]</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=5a9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9h OCA], [https://pdbe.org/5a9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9h RCSB], [https://www.ebi.ac.uk/pdbsum/5a9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9h ProSAT]</span></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=5a9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9h OCA], [http://pdbe.org/5a9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a9h RCSB], [http://www.ebi.ac.uk/pdbsum/5a9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/S15A2_RAT S15A2_RAT]] Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides. | + | [https://www.uniprot.org/uniprot/S15A2_RAT S15A2_RAT] Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beale, J H]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Newstead, S]] | + | [[Category: Beale JH]] |
| - | [[Category: Extracellular domain]] | + | [[Category: Newstead S]] |
| - | [[Category: Mf]]
| + | |
| - | [[Category: Pept2]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
S15A2_RAT Proton-coupled intake of oligopeptides of 2 to 4 amino acids with a preference for dipeptides.
Publication Abstract from PubMed
Mammals obtain nitrogen via the uptake of di- and tri-peptides in the gastrointestinal tract through the action of PepT1 and PepT2, which are members of the POT family of proton-coupled oligopeptide transporters. PepT1 and PepT2 also play an important role in drug transport in the human body. Recent crystal structures of bacterial homologs revealed a conserved peptide-binding site and mechanism of transport. However, a key structural difference exists between bacterial and mammalian homologs with only the latter containing a large extracellular domain, the function of which is currently unknown. Here, we present the crystal structure of the extracellular domain from both PepT1 and PepT2 that reveal two immunoglobulin-like folds connected in tandem, providing structural insight into mammalian peptide transport. Functional and biophysical studies demonstrate that these domains interact with the intestinal protease trypsin, suggesting a role in clustering proteolytic activity to the site of peptide transport in eukaryotic cells.
Crystal Structures of the Extracellular Domain from PepT1 and PepT2 Provide Novel Insights into Mammalian Peptide Transport.,Beale JH, Parker JL, Samsudin F, Barrett AL, Senan A, Bird LE, Scott D, Owens RJ, Sansom MS, Tucker SJ, Meredith D, Fowler PW, Newstead S Structure. 2015 Aug 27. pii: S0969-2126(15)00322-6. doi:, 10.1016/j.str.2015.07.016. PMID:26320580[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Beale JH, Parker JL, Samsudin F, Barrett AL, Senan A, Bird LE, Scott D, Owens RJ, Sansom MS, Tucker SJ, Meredith D, Fowler PW, Newstead S. Crystal Structures of the Extracellular Domain from PepT1 and PepT2 Provide Novel Insights into Mammalian Peptide Transport. Structure. 2015 Aug 27. pii: S0969-2126(15)00322-6. doi:, 10.1016/j.str.2015.07.016. PMID:26320580 doi:http://dx.doi.org/10.1016/j.str.2015.07.016
|
