This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4bwb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='4bwb' size='340' side='right'caption='[[4bwb]], [[Resolution|resolution]] 3.57&Aring;' scene=''>
<StructureSection load='4bwb' size='340' side='right'caption='[[4bwb]], [[Resolution|resolution]] 3.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4bwb]] is a 4 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=4BWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BWB FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4bwb]] 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=4BWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BWB FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zev|3zev]], [[4buo|4buo]], [[4bv0|4bv0]]</td></tr>
+
</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=4bwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwb OCA], [https://pdbe.org/4bwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bwb RCSB], [https://www.ebi.ac.uk/pdbsum/4bwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwb 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=4bwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwb OCA], [http://pdbe.org/4bwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bwb RCSB], [http://www.ebi.ac.uk/pdbsum/4bwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwb ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[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.
+
[[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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4bwb" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Neurotensin receptor|Neurotensin receptor]]
*[[Neurotensin receptor|Neurotensin receptor]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Balada, S]]
+
[[Category: Rattus norvegicus]]
-
[[Category: Batyuk, A]]
+
[[Category: Balada S]]
-
[[Category: Egloff, P]]
+
[[Category: Batyuk A]]
-
[[Category: Heine, P]]
+
[[Category: Egloff P]]
-
[[Category: Hillenbrand, M]]
+
[[Category: Heine P]]
-
[[Category: Mittl, P]]
+
[[Category: Hillenbrand M]]
-
[[Category: Plueckthun, A]]
+
[[Category: Mittl P]]
-
[[Category: Schlinkmann, K M]]
+
[[Category: Plueckthun A]]
-
[[Category: Scott, D J]]
+
[[Category: Schlinkmann KM]]
-
[[Category: G protein coupled receptor]]
+
[[Category: Scott DJ]]
-
[[Category: Membrane protein]]
+
-
[[Category: Signaling protein]]
+

Revision as of 17:12, 7 September 2022

Structure of Evolved Agonist-bound Neurotensin Receptor 1 Mutant without Lysozyme Fusion

PDB ID 4bwb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bwb"
Personal tools