1sp7: Difference between revisions

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-[[Image:1sp7.png|left|200px]]
-<!--
+==Structure of the Cys-rich C-terminal domain of Hydra minicollagen==
-The line below this paragraph, containing "STRUCTURE_1sp7", creates the "Structure Box" on the page.
+<StructureSection load='1sp7' size='340' side='right'caption='[[1sp7]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1sp7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydra_sp. Hydra sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SP7 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=1sp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp7 OCA], [https://pdbe.org/1sp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sp7 RCSB], [https://www.ebi.ac.uk/pdbsum/1sp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp7 ProSAT]</span></td></tr>
-{{STRUCTURE_1sp7|  PDB=1sp7  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q00484_9CNID Q00484_9CNID]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A high-precision solution structure of the C-terminal minicollagen cysteine rich domain of Hydra has been determined using modern heteronuclear and weak alignment NMR techniques at natural isotope abundance. The domain consists of only 24 amino acids, six of which are prolines and six are cysteines bonded in disulfide bridges that constrain the structure into a new fold. The redox equilibrium of the structure has been characterized from a titration with glutathione. No local native structures are detectable in the reduced form. Thus, oxidation and folding are tightly coupled.
-===Structure of the Cys-rich C-terminal domain of Hydra minicollagen===
+Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation.,Meier S, Haussinger D, Pokidysheva E, Bachinger HP, Grzesiek S FEBS Lett. 2004 Jul 2;569(1-3):112-6. PMID:15225618<ref>PMID:15225618</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1sp7" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15225618}}, adds the Publication Abstract to the page
+*[[Collagen 3D structures|Collagen 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15225618 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15225618}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Hydra sp]]
-[[1sp7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP7 OCA].
+[[Category: Large Structures]]
+[[Category: Bachinger HP]]
-==Reference==
+[[Category: Grzesiek S]]
-<ref group="xtra">PMID:15225618</ref><ref group="xtra">PMID:15123641</ref><references group="xtra"/>
+[[Category: Haussinger D]]
-[[Category: Bachinger, H P.]]
+[[Category: Meier S]]
-[[Category: Grzesiek, S.]]
+[[Category: Pokidysheva E]]
-[[Category: Haussinger, D.]]
-[[Category: Meier, S.]]
-[[Category: Pokidysheva, E.]]
-[[Category: Cysteine-rich]]
-[[Category: Disulfide bond]]
-[[Category: Proline-rich]]
-[[Category: Structural protein]]