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[[Image:1kpb.gif|left|200px]]


{{Structure
==PKCI-1-APO==
|PDB= 1kpb |SIZE=350|CAPTION= <scene name='initialview01'>1kpb</scene>, resolution 2.0&Aring;
<StructureSection load='1kpb' size='340' side='right'caption='[[1kpb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE= <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>
== Structural highlights ==
|LIGAND=
<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>
|ACTIVITY=
</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>
|GENE= HPKCI-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpb OCA], [http://www.ebi.ac.uk/pdbsum/1kpb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kpb RCSB]</span>
[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>


'''PKCI-1-APO'''
==See Also==
 
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1KPB is a [[Single protein]] structure of sequence 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=1KPB OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/8643579 8643579]
[[Category: Homo sapiens]]
[[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 Mar 30 21:51:42 2008''

Latest revision as of 10:26, 14 February 2024

PKCI-1-APOPKCI-1-APO

Structural highlights

1kpb is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

See Also

1kpb, resolution 2.00Å

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