View source for 2jp1


==Solution structure of the alternative conformation of XCL1/Lymphotactin==
<StructureSection load='2jp1' size='340' side='right'caption='[[2jp1]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jp1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JP1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=2jp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jp1 OCA], [https://pdbe.org/2jp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jp1 RCSB], [https://www.ebi.ac.uk/pdbsum/2jp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jp1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XCL1_HUMAN XCL1_HUMAN] Chemotactic activity for lymphocytes but not for monocytes or neutrophils.
== 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/jp/2jp1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2jp1 ConSurf].
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== Publication Abstract from PubMed ==
Proteins often have multiple functional states, which might not always be accommodated by a single fold. Lymphotactin (Ltn) adopts two distinct structures in equilibrium, one corresponding to the canonical chemokine fold consisting of a monomeric three-stranded beta-sheet and carboxyl-terminal helix. The second Ltn structure solved by NMR reveals a dimeric all-beta-sheet arrangement with no similarity to other known proteins. In physiological solution conditions, both structures are significantly populated and interconvert rapidly. Interconversion replaces long-range interactions that stabilize the chemokine fold with an entirely new set of tertiary and quaternary contacts. The chemokine-like Ltn conformation is a functional XCR1 agonist, but fails to bind heparin. In contrast, the alternative structure binds glycosaminoglycans with high affinity but fails to activate XCR1. Because each structural species displays only one of the two functional properties essential for activity in vivo, the conformational equilibrium is likely to be essential for the biological activity of lymphotactin. These results demonstrate that the functional repertoire and regulation of a single naturally occurring amino acid sequence can be expanded by access to a set of highly dissimilar native-state structures.

Interconversion between two unrelated protein folds in the lymphotactin native state.,Tuinstra RL, Peterson FC, Kutlesa S, Elgin ES, Kron MA, Volkman BF Proc Natl Acad Sci U S A. 2008 Apr 1;105(13):5057-62. Epub 2008 Mar 25. PMID:18364395<ref>PMID:18364395</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Peterson FC]]
[[Category: Tuinstra RL]]
[[Category: Volkman BF]]