2lcs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:55, 1 May 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Yeast Nbp2p SH3 domain in complex with a peptide from Ste20p==
==Yeast Nbp2p SH3 domain in complex with a peptide from Ste20p==
-
<StructureSection load='2lcs' size='340' side='right'caption='[[2lcs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+
<StructureSection load='2lcs' size='340' side='right'caption='[[2lcs]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2lcs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LCS FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2lcs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LCS FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NBP2, YDR162C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=2lcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lcs OCA], [https://pdbe.org/2lcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lcs RCSB], [https://www.ebi.ac.uk/pdbsum/2lcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lcs ProSAT]</span></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=2lcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lcs OCA], [https://pdbe.org/2lcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lcs RCSB], [https://www.ebi.ac.uk/pdbsum/2lcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lcs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/NBP2_YEAST NBP2_YEAST]] Negatively regulates the high-osmolarity glycerol (HOG) pathway through its negative regulation of the HOG1 kinase activity. Mediates the binding between the PTC1 phosphatase and the PBS2 MAP/ERK kinase (MEK). With PTC1, regulates endoplasmic reticulum inheritance through the cell wall integrity (CWI) MAPK pathway by modulating the MAPK, SLT2.<ref>PMID:14573466</ref> <ref>PMID:14685261</ref> <ref>PMID:16977319</ref> [[https://www.uniprot.org/uniprot/STE20_YEAST STE20_YEAST]] MAP4K component of the MAPK pathway required for the mating pheromone response, haploid invasive growth and diploid pseudohyphal development. Links the pheromone response G-protein beta gamma subunits to downstream signaling components. Needed for mating in haploid cells, induction of a mating-specific gene FUS1, induction of mating-specific morphologies, and pheromone-induced proliferation arrest. Required for the regulation of the actin polarization and bud emergence during cell cycle in G1. Involved in the high osmolarity glycerol (HOG) response. Phosphorylates 'Thr-307' and 'Ser-302' or 'Ser-306' of STE11 and 'Ser-357' of MYO3. Phosphorylates histone H2B to form H2BS10ph during meiosis and H(2)O(2)-induced apoptosis. Its interaction with CDC42 is required for both invasive growth and the formation of pseudohyphae. Its interaction with STE4 is required for the pheromone signaling.<ref>PMID:1464311</ref> <ref>PMID:8421676</ref> <ref>PMID:7608157</ref> <ref>PMID:9003780</ref> <ref>PMID:8722766</ref> <ref>PMID:8643578</ref> <ref>PMID:9009270</ref> <ref>PMID:9388196</ref> <ref>PMID:9742399</ref> <ref>PMID:9428767</ref> <ref>PMID:10562285</ref> <ref>PMID:10837245</ref> <ref>PMID:10970855</ref> <ref>PMID:11003652</ref> <ref>PMID:11940652</ref> <ref>PMID:12686605</ref> <ref>PMID:12588977</ref> <ref>PMID:15652479</ref> <ref>PMID:15970663</ref> <ref>PMID:15743816</ref>
+
[https://www.uniprot.org/uniprot/NBP2_YEAST NBP2_YEAST] Negatively regulates the high-osmolarity glycerol (HOG) pathway through its negative regulation of the HOG1 kinase activity. Mediates the binding between the PTC1 phosphatase and the PBS2 MAP/ERK kinase (MEK). With PTC1, regulates endoplasmic reticulum inheritance through the cell wall integrity (CWI) MAPK pathway by modulating the MAPK, SLT2.<ref>PMID:14573466</ref> <ref>PMID:14685261</ref> <ref>PMID:16977319</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The yeast Nbp2p SH3 and Bem1p SH3b domains bind certain target peptides with similar high affinities, yet display vastly different affinities for other targets. To investigate this unusual behavior, we have solved the structure of the Nbp2p SH3-Ste20 peptide complex and compared it with the previously determined structure of the Bem1p SH3b bound to the same peptide. Although the Ste20 peptide interacts with both domains in a structurally similar manner, extensive in vitro studies with domain and peptide mutants revealed large variations in interaction strength across the binding interface of the two complexes. Whereas the Nbp2p SH3 made stronger contacts with the peptide core RXXPXXP motif, the Bem1p SH3b domain made stronger contacts with residues flanking the core motif. Remarkably, this modulation of local binding energetics can explain the distinct and highly nuanced binding specificities of these two domains.
+
-
 
+
-
Distinct Peptide Binding Specificities of Src Homology 3 (SH3) Protein Domains Can Be Determined by Modulation of Local Energetics across the Binding Interface.,Gorelik M, Davidson AR J Biol Chem. 2012 Mar 16;287(12):9168-77. Epub 2012 Jan 25. PMID:22277653<ref>PMID:22277653</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 2lcs" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Non-specific serine/threonine protein kinase]]
+
[[Category: Saccharomyces cerevisiae S288C]]
-
[[Category: Davidson, A R]]
+
[[Category: Davidson AR]]
-
[[Category: Gorelik, M]]
+
[[Category: Gorelik M]]
-
[[Category: Adaptor]]
+
-
[[Category: Signaling protein]]
+
-
[[Category: Transferase]]
+

Current revision

Yeast Nbp2p SH3 domain in complex with a peptide from Ste20p

PDB ID 2lcs

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools