1kpb: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1kpb.gif|left|200px]]<br /><applet load="1kpb" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1kpb, resolution 2.0&Aring;" />
-'''PKCI-1-APO'''<br />
-==Overview==
+==PKCI-1-APO==
-The three-dimensional structure of protein kinase C interacting protein 1, (PKCI-1) has been solved to high resolution by x-ray crystallography using, single isomorphous replacement with anomalous scattering. The gene, encoding human PKCI-1 was cloned from a cDNA library by using a partial, sequence obtained from interactions identified in the yeast two-hybrid, system between PKCI-1 and the regulatory domain of protein kinase C-beta., The PKCI-1 protein was expressed in Pichia pastoris as a dimer of two, 13.7-kDa polypeptides. PKCI-1 is a member of the HIT family of proteins, shown by sequence identity to be conserved in a broad range of organisms, including mycoplasma, plants, and humans. Despite the ubiquity of this, protein sequence in nature, no distinct function has been shown for the, protein product in vitro or in vivo. The PKCI-1 protomer has an alpha+beta, meander fold containing a five-stranded antiparallel sheet and two, helices. Two protomers come together to form a 10-stranded antiparallel, sheet with extensive contacts between a helix and carboxy terminal amino, acids of a protomer with the corresponding amino acids in the other, protomer. PKCI-1 has been shown to interact specifically with zinc. The, three-dimensional structure has been solved in the presence and absence of, zinc and in two crystal forms. The structure of human PKCI-1 provides a, model of this family of proteins which suggests a stable fold conserved, throughout nature.
+<StructureSection load='1kpb' size='340' side='right'caption='[[1kpb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1kpb]] is a 2 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=1KPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KPB 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&#8491;</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=1kpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpb OCA], [https://pdbe.org/1kpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kpb RCSB], [https://www.ebi.ac.uk/pdbsum/1kpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kpb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HINT1_HUMAN HINT1_HUMAN] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity).
+== 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/kp/1kpb_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=1kpb ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-KPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Known structural/functional Sites: <scene name='pdbsite=ZNA:Triad+Of+Histidines+Potentially+Involved+In+Zn+Coordination'>ZNA</scene> and <scene name='pdbsite=ZNB:Triad+Of+Histidines+Potentially+Involved+In+Zn+Coordination'>ZNB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPB OCA].
+*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins., Lima CD, Klein MG, Weinstein IB, Hendrickson WA, Proc Natl Acad Sci U S A. 1996 May 28;93(11):5357-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8643579 8643579]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Hendrickson, W.A.]]
+[[Category: Hendrickson WA]]
-[[Category: Klein, M.G.]]
+[[Category: Klein MG]]
-[[Category: Lima, C.D.]]
+[[Category: Lima CD]]
-[[Category: Weinstein, I.B.]]
+[[Category: Weinstein IB]]
-[[Category: pkc]]
-[[Category: pkci-1]]
-[[Category: signal transduction]]
-[[Category: zinc binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:52:57 2008''