1hum: Difference between revisions

Revision as of 08:43, 1 July 2008

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File:1hum.png

Template:STRUCTURE 1hum

SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMERSOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER

Template:ABSTRACT PUBMED 8134838

About this StructureAbout this Structure

1HUM is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR., Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM, Science. 1994 Mar 25;263(5154):1762-7. PMID:8134838

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

OCA

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-'''SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER'''
+===SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER===
-==Overview==
+<!--
-The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of approximately 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interface is formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.
+The line below this paragraph, {{ABSTRACT_PUBMED_8134838}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8134838 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8134838}}
 ==About this Structure==
-HUM 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=1HUM OCA].
+HUM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HUM OCA].
 ==Reference==
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 [[Category: Gronenborn, A M.]]
 [[Category: Lodi, P J.]]
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