4bv0: Difference between revisions

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-{{STRUCTURE_4bv0|  PDB=4bv0  |  SCENE=  }}
-===High Resolution Structure of Evolved Agonist-bound Neurotensin Receptor 1 Mutant without Lysozyme Fusion===
-{{ABSTRACT_PUBMED_24453215}}
-==Function==
+==High Resolution Structure of Evolved Agonist-bound Neurotensin Receptor 1 Mutant without Lysozyme Fusion==
-[[http://www.uniprot.org/uniprot/NTR1_RAT NTR1_RAT]] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. [[http://www.uniprot.org/uniprot/NEUT_RAT NEUT_RAT]] Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle.
+<StructureSection load='4bv0' size='340' side='right'caption='[[4bv0]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4bv0]] is a 4 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=4BV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BV0 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#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=4bv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bv0 OCA], [https://pdbe.org/4bv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bv0 RCSB], [https://www.ebi.ac.uk/pdbsum/4bv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bv0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NTR1_RAT NTR1_RAT] Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Crystallography has advanced our understanding of G protein-coupled receptors, but low expression levels and instability in solution have limited structural insights to very few selected members of this large protein family. Using neurotensin receptor 1 (NTR1) as a proof of principle, we show that two directed evolution technologies that we recently developed have the potential to overcome these problems. We purified three neurotensin-bound NTR1 variants from Escherichia coli and determined their X-ray structures at up to 2.75 A resolution using vapor diffusion crystallization experiments. A crystallized construct was pharmacologically characterized and exhibited ligand-dependent signaling, internalization, and wild-type-like agonist and antagonist affinities. Our structures are fully consistent with all biochemically defined ligand-contacting residues, and they represent an inactive NTR1 state at the cytosolic side. They exhibit significant differences to a previously determined NTR1 structure (Protein Data Bank ID code 4GRV) in the ligand-binding pocket and by the presence of the amphipathic helix 8. A comparison of helix 8 stability determinants between NTR1 and other crystallized G protein-coupled receptors suggests that the occupancy of the canonical position of the amphipathic helix is reduced to various extents in many receptors, and we have elucidated the sequence determinants for a stable helix 8. Our analysis also provides a structural rationale for the long-known effects of C-terminal palmitoylation reactions on G protein-coupled receptor signaling, receptor maturation, and desensitization.
-==About this Structure==
+Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli.,Egloff P, Hillenbrand M, Klenk C, Batyuk A, Heine P, Balada S, Schlinkmann KM, Scott DJ, Schutz M, Pluckthun A Proc Natl Acad Sci U S A. 2014 Jan 22. PMID:24453215<ref>PMID:24453215</ref>
-[[4bv0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BV0 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:024453215</ref><references group="xtra"/><references/>
+</div>
-[[Category: Balada, S.]]
+<div class="pdbe-citations 4bv0" style="background-color:#fffaf0;"></div>
-[[Category: Batyuk, A.]]
-[[Category: Egloff, P.]]
+==See Also==
-[[Category: Heine, P.]]
+*[[Neurotensin receptor|Neurotensin receptor]]
-[[Category: Hillenbrand, M.]]
+== References ==
-[[Category: Mittl, P.]]
+<references/>
-[[Category: Plueckthun, A.]]
+__TOC__
-[[Category: Schlinkmann, K M.]]
+</StructureSection>
-[[Category: Schuetz, M.]]
+[[Category: Large Structures]]
-[[Category: Scott, D J.]]
+[[Category: Rattus norvegicus]]
-[[Category: G protein coupled receptor]]
+[[Category: Balada S]]
-[[Category: Membrane protein]]
+[[Category: Batyuk A]]
-[[Category: Signaling protein]]
+[[Category: Egloff P]]
+[[Category: Heine P]]
+[[Category: Hillenbrand M]]
+[[Category: Mittl P]]
+[[Category: Plueckthun A]]
+[[Category: Schlinkmann KM]]
+[[Category: Schuetz M]]
+[[Category: Scott DJ]]