2jyp

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[[Image:2jyp.png|left|200px]]
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==Coordinates for lowest energy structure of Aragonite protein-7, C-terminal domain==
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<StructureSection load='2jyp' size='340' side='right' caption='[[2jyp]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2jyp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JYP FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jyp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jyp RCSB], [http://www.ebi.ac.uk/pdbsum/2jyp PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The RING or Really Interesting New Gene represents a family of eukaryotic sequences that bind Zn (II) ions and participate in intracellular processes involving protein-protein interaction. Although found in over 400 different proteins, very little is known regarding the structure-function properties of these domains because of the aggregation problems associated with RING sequences. To augment this data set, we report an unusual 36 AA C-terminal sequence of an extracellular matrix mollusk shell protein, AP7, that exhibits partial homology to the RING family. This Cys, His-containing sequence, termed AP7C, binds Zn (II) and other multivalent ions, but does not utilize a tetracoordinate complexation scheme for binding such as that found in Zn (II) finger polypeptides. Moreover, unlike Zn (II) finger and RING domains, this 36 AA can fold into a relatively stable structure in the absence of Zn (II). This folded structure consists of three short helical segments (A, B, and C), with segments A and B separated by a 4 AA type I beta-turn region and segments B and C separated by a 7 AA loop-like region. Interestingly, the putative RING-like region, -RRPFHECALCYSI-, experiences slow conformational exchange between two structural states in solution, most likely in response to imido ring interconversion at P8 and P21. Poisson-Boltzmann solvation calculations reveal that the AP7C molecular surface possesses a cationic region near its N-terminus, which lies adjacent to the 30 AA mineral modification domain in the AP7 protein. Given that the AP7C sequence does not influence mineralization, it is probable that this cationic pseudo-RING region is utilized by the AP7 protein for other tasks such as protein-protein interaction within the mollusk shell matrix.
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{{STRUCTURE_2jyp| PDB=2jyp | SCENE= }}
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Identification and Structural Characterization of an Unusual RING-Like Sequence within an Extracellular Biomineralization Protein, AP7.,Collino S, Kim IW, Evans JS Biochemistry. 2008 Mar 25;47(12):3745-55. Epub 2008 Feb 26. PMID:18298090<ref>PMID:18298090</ref>
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===Coordinates for lowest energy structure of Aragonite protein-7, C-terminal domain===
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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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{{ABSTRACT_PUBMED_18298090}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2jyp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JYP OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:018298090</ref><references group="xtra"/>
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[[Category: Collino, S.]]
[[Category: Collino, S.]]
[[Category: Evans, J.]]
[[Category: Evans, J.]]

Revision as of 06:49, 9 June 2014

Coordinates for lowest energy structure of Aragonite protein-7, C-terminal domain

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