1nzv

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[[Image:1nzv.png|left|200px]]
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==Crystal Structure of Src SH2 domain bound to doubly phosphorylated peptide PQpYIpYVPA==
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<StructureSection load='1nzv' size='340' side='right' caption='[[1nzv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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[[1nzv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Rsvsr Rsvsr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZV OCA]. <br>
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<b>Related:</b> [[1iso|1iso]], [[1kc2|1kc2]], [[1nzl|1nzl]], [[1sps|1sps]]<br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nz/1nzv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
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Recruitment of the Src kinase to the activated form of the platelet-derived growth factor (PDGF) receptor involves recognition of a unique sequence motif in the juxtamembrane region of the receptor by the Src homology 2 (SH2) domain of the enzyme. This motif contains two phosphotyrosine residues separated by one residue (sequence pYIpYV where pY indicates a phosphotyrosine). Here, we provide the thermodynamic and structural basis for the binding of this motif by the Src SH2 domain. We show that the second phosphorylation event increases the free energy window for specific interaction and that the physiological target is exquisitely designed for the task of recruiting specifically an SH2 domain which otherwise demonstrates very little intrinsic ability to discriminate sequences C-terminal to the first phosphorylation event. Surprisingly, we show that water plays a role in the recognition process.
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{{STRUCTURE_1nzv| PDB=1nzv | SCENE= }}
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Structural and thermodynamic basis for the interaction of the Src SH2 domain with the activated form of the PDGF beta-receptor.,Lubman OY, Waksman G J Mol Biol. 2003 May 2;328(3):655-68. PMID:12706723<ref>PMID:12706723</ref>
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===Crystal Structure of Src SH2 domain bound to doubly phosphorylated peptide PQpYIpYVPA===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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{{ABSTRACT_PUBMED_12706723}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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[[1nzv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus_(strain_schmidt-ruppin) Rous sarcoma virus (strain schmidt-ruppin)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZV OCA].
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[[Category: Rsvsr]]
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==Reference==
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<ref group="xtra">PMID:012706723</ref><references group="xtra"/>
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Lubman, O Y.]]
[[Category: Lubman, O Y.]]

Revision as of 05:24, 30 April 2014

Crystal Structure of Src SH2 domain bound to doubly phosphorylated peptide PQpYIpYVPA

1nzv, resolution 2.10Å

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