1sps

From Proteopedia

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Revision as of 07:35, 22 September 2021

BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS

Structural highlights

1sps is a 6 chain structure with sequence from [1] and Rous sarcoma virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SRC_RSVSA] This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. [MT_POVHA] Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with Ppp2/PP2A the Src tyrosine kinase component Fyn, thereby activating its kinase activity. In turn, MT becomes phosphorylated and mediates signal transduction pathways leading to cell cycle progression and cell division. MT plays also a role in regulation of early and late gene expression as well as viral DNA replication (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide has been determined at 2.7 A resolution by X-ray diffraction. The peptide binds in an extended conformation and makes primary interactions with the SH2 domain at six central residues: PQ(pY)EEI. The phosphotyrosine and the isoleucine are tightly bound by two well-defined pockets on the protein surface, resulting in a complex that resembles a two-pronged plug engaging a two-holed socket. The glutamate residues are in solvent-exposed environments in the vicinity of basic side chains of the SH2 domain, and the two N-terminal residues cap the phosphotyrosine-binding site. The crystal structure of Src SH2 in the absence of peptide has been determined at 2.5 A resolution, and comparison with the structure of the high affinity complex reveals only localized and relatively small changes.

Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms.,Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J Cell. 1993 Mar 12;72(5):779-90. PMID:7680960^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell. 1993 Mar 12;72(5):779-90. PMID:7680960

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sps"

Categories: Large Structures | Rous sarcoma virus | Kuriyan, J | Waksman, G

@@ Line 3: / Line 3: @@
 <StructureSection load='1sps' size='340' side='right'caption='[[1sps]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1sps]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SPS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1sps]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ ] and [https://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SPS FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></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=1sps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sps OCA], [http://pdbe.org/1sps PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sps RCSB], [http://www.ebi.ac.uk/pdbsum/1sps PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sps 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=1sps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sps OCA], [https://pdbe.org/1sps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sps RCSB], [https://www.ebi.ac.uk/pdbsum/1sps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sps ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SRC_RSVSA SRC_RSVSA]] This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. [[http://www.uniprot.org/uniprot/MT_POVHA MT_POVHA]] Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with Ppp2/PP2A the Src tyrosine kinase component Fyn, thereby activating its kinase activity. In turn, MT becomes phosphorylated and mediates signal transduction pathways leading to cell cycle progression and cell division. MT plays also a role in regulation of early and late gene expression as well as viral DNA replication (By similarity).
+[[https://www.uniprot.org/uniprot/SRC_RSVSA SRC_RSVSA]] This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro. [[https://www.uniprot.org/uniprot/MT_POVHA MT_POVHA]] Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with Ppp2/PP2A the Src tyrosine kinase component Fyn, thereby activating its kinase activity. In turn, MT becomes phosphorylated and mediates signal transduction pathways leading to cell cycle progression and cell division. MT plays also a role in regulation of early and late gene expression as well as viral DNA replication (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1sps

From Proteopedia

Revision as of 07:35, 22 September 2021

BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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