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.


1spr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1spr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1spr, resolution 2.5&Aring;" /> '''BINDING OF A HIGH AFF...)
Current revision (08:32, 14 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1spr.gif|left|200px]]<br /><applet load="1spr" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1spr, resolution 2.5&Aring;" />
 
-
'''BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS'''<br />
 
-
==Overview==
+
==BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS==
-
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.
+
<StructureSection load='1spr' size='340' side='right'caption='[[1spr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1spr]] is a 4 chain structure with sequence from [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=1SPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SPR 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]] 2.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1spr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spr OCA], [https://pdbe.org/1spr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1spr RCSB], [https://www.ebi.ac.uk/pdbsum/1spr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1spr ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sp/1spr_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1spr ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1SPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SPR OCA].
+
*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7680960 7680960]
+
[[Category: Large Structures]]
[[Category: Rous sarcoma virus]]
[[Category: Rous sarcoma virus]]
-
[[Category: Single protein]]
+
[[Category: Kuriyan J]]
-
[[Category: Kuriyan, J.]]
+
[[Category: Waksman G]]
-
[[Category: Waksman, G.]]
+
-
[[Category: PO4]]
+
-
[[Category: transferase(phosphotransferase)]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:33:08 2007''
+

Current revision

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

PDB ID 1spr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools