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1h26

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{{Seed}}
 
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[[Image:1h26.png|left|200px]]
 
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==CDK2/CyclinA in complex with an 11-residue recruitment peptide from p53==
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The line below this paragraph, containing "STRUCTURE_1h26", creates the "Structure Box" on the page.
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<StructureSection load='1h26' size='340' side='right'caption='[[1h26]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1h26]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H26 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.24&#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=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
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{{STRUCTURE_1h26| PDB=1h26 | SCENE= }}
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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=1h26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h26 OCA], [https://pdbe.org/1h26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h26 RCSB], [https://www.ebi.ac.uk/pdbsum/1h26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h26 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|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/h2/1h26_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/main_output.php?pdb_ID=1h26 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Progression through S phase of the eukaryotic cell cycle is regulated by the action of the cyclin dependent protein kinase 2 (CDK2) in association with cyclin A. CDK2/cyclin A phosphorylates numerous substrates. Substrate specificity often employs a dual recognition strategy in which the sequence flanking the phospho-acceptor site (Ser.Pro.X.Arg/Lys) is recognized by CDK2, while the cyclin A component of the complex contains a hydrophobic site that binds Arg/Lys.X.Leu ("RXL" or "KXL") substrate recruitment motifs. To determine additional sequence specificity motifs around the RXL sequence, we have performed X-ray crystallographic studies at 2.3 A resolution and isothermal calorimetry measurements on complexes of phospho-CDK2/cyclin A with a recruitment peptide derived from E2F1 and with shorter 11-mer peptides from p53, pRb, p27, E2F1, and p107. The results show that the cyclin recruitment site accommodates a second hydrophobic residue either immediately C-terminal or next adjacent to the leucine of the "RXL" motif and that this site makes important contributions to the recruitment peptide recognition. The arginine of the RXL motif contacts a glutamate, Glu220, on the cyclin. In those substrates that contain a KXL motif, no ionic interactions are observed with the lysine. The sequences N-terminal to the "RXL" motif of the individual peptides show no conservation, but nevertheless make common contacts to the cyclin through main chain interactions. Thus, the recruitment site is able to recognize diverse but conformationally constrained target sequences. The observations have implications for the further identification of physiological substrates of CDK2/cyclin A and the design of specific inhibitors.
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===CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P53===
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Specificity determinants of recruitment peptides bound to phospho-CDK2/cyclin A.,Lowe ED, Tews I, Cheng KY, Brown NR, Gul S, Noble ME, Gamblin SJ, Johnson LN Biochemistry. 2002 Dec 31;41(52):15625-34. PMID:12501191<ref>PMID:12501191</ref>
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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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<div class="pdbe-citations 1h26" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12501191}}, adds the Publication Abstract to the page
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*[[Cyclin 3D structures|Cyclin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12501191 is the PubMed ID number.
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*[[Cyclin-dependent kinase 3D structures|Cyclin-dependent kinase 3D structures]]
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-->
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== References ==
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{{ABSTRACT_PUBMED_12501191}}
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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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1H26 is a 5 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H26 OCA].
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==Reference==
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<ref group="xtra">PMID:12501191</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Brown, N R.]]
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[[Category: Large Structures]]
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[[Category: Cheng, K Y.]]
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[[Category: Brown NR]]
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[[Category: Gamblin, S.]]
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[[Category: Cheng KY]]
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[[Category: Gul, S.]]
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[[Category: Gamblin S]]
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[[Category: Johnson, L N.]]
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[[Category: Gul S]]
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[[Category: Lowe, E D.]]
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[[Category: Johnson LN]]
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[[Category: Noble, M E.M.]]
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[[Category: Lowe ED]]
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[[Category: Tews, I.]]
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[[Category: Noble MEM]]
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[[Category: Cdk2]]
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[[Category: Tews I]]
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[[Category: Cell cycle]]
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[[Category: Cyclin]]
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[[Category: Peptide specificity]]
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[[Category: Protein kinase]]
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[[Category: Recruitment]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:28:19 2009''
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Current revision

CDK2/CyclinA in complex with an 11-residue recruitment peptide from p53

PDB ID 1h26

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