3n94

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[[Image:3n94.png|left|200px]]
 
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{{STRUCTURE_3n94| PDB=3n94 | SCENE= }}
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==Crystal structure of human pituitary adenylate cyclase 1 Receptor-short N-terminal extracellular domain==
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<StructureSection load='3n94' size='340' side='right'caption='[[3n94]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3n94]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N94 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3n94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n94 OCA], [https://pdbe.org/3n94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n94 RCSB], [https://www.ebi.ac.uk/pdbsum/3n94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n94 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/PACR_HUMAN PACR_HUMAN] This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pituitary adenylate cyclase activating polypeptide (PACAP) is a member of the PACAP/glucagon family of peptide hormones, which controls many physiological functions in the immune, nervous, endocrine, and muscular systems. It activates adenylate cyclase by binding to its receptor, PAC1R, a member of class B G-protein coupled receptors (GPCR). Crystal structures of a number of Class B GPCR extracellular domains (ECD) bound to their respective peptide hormones have revealed a consensus mechanism of hormone binding. However, the mechanism of how PACAP binds to its receptor remains controversial as an NMR structure of the PAC1R ECD/PACAP complex reveals a different topology of the ECD and a distinct mode of ligand recognition. Here we report a 1.9 A crystal structure of the PAC1R ECD, which adopts the same fold as commonly observed for other members of Class B GPCR. Binding studies and cell-based assays with alanine-scanned peptides and mutated receptor support a model that PAC1R uses the same conserved fold of Class B GPCR ECD for PACAP binding, thus unifying the consensus mechanism of hormone binding for this family of receptors.
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===Crystal structure of human pituitary adenylate cyclase 1 Receptor-short N-terminal extracellular domain===
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Crystal Structure of the PAC1R Extracellular Domain Unifies a Consensus Fold for Hormone Recognition by Class B G-Protein Coupled Receptors.,Kumar S, Pioszak A, Zhang C, Swaminathan K, Xu HE PLoS One. 2011;6(5):e19682. Epub 2011 May 19. PMID:21625560<ref>PMID:21625560</ref>
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{{ABSTRACT_PUBMED_21625560}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 3n94" style="background-color:#fffaf0;"></div>
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[[3n94]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N94 OCA].
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==See Also==
==See Also==
*[[Hormone|Hormone]]
*[[Hormone|Hormone]]
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*[[Maltose-binding protein|Maltose-binding protein]]
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:021625560</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Escherichia coli k-12]]
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[[Category: Escherichia coli K-12]]
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[[Category: Kumar, S.]]
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[[Category: Homo sapiens]]
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[[Category: Pioszak, A A.]]
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[[Category: Large Structures]]
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[[Category: Swaminathan, K.]]
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[[Category: Kumar S]]
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[[Category: Xu, H E.]]
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[[Category: Pioszak AA]]
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[[Category: G-protein coupled receptor]]
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[[Category: Swaminathan K]]
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[[Category: Mbp fusion protein]]
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[[Category: Xu HE]]
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[[Category: Membrane receptor]]
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[[Category: Peptide hormone receptor]]
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Current revision

Crystal structure of human pituitary adenylate cyclase 1 Receptor-short N-terminal extracellular domain

PDB ID 3n94

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