1ikm: Difference between revisions

Revision as of 13:24, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ikm.png

Template:STRUCTURE 1ikm

NMR STUDY OF MONOMERIC HUMAN INTERLEUKIN-8 (30 STRUCTURES)NMR STUDY OF MONOMERIC HUMAN INTERLEUKIN-8 (30 STRUCTURES)

Template:ABSTRACT PUBMED 7548056

About this StructureAbout this Structure

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

ReferenceReference

1H NMR solution structure of an active monomeric interleukin-8., Rajarathnam K, Clark-Lewis I, Sykes BD, Biochemistry. 1995 Oct 10;34(40):12983-90. PMID:7548056

Page seeded by OCA on Tue Jul 1 13:24:00 2008

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

OCA

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 {{STRUCTURE_1ikm|  PDB=1ikm  |  SCENE=  }}
-'''NMR STUDY OF MONOMERIC HUMAN INTERLEUKIN-8 (30 STRUCTURES)'''
+===NMR STUDY OF MONOMERIC HUMAN INTERLEUKIN-8 (30 STRUCTURES)===
-==Overview==
+<!--
-The solution structure of a monomeric form of interleukin-8 (IL-8) has been solved using 1H NMR spectroscopy. The chemically synthesized nonnatural analog [IL-8 (4-72) L25 NH--&gt;NCH3] has the same activity as that of native IL-8. Thirty structures were generated using the hybrid distance geometry and simulated annealing protocol using the program X-PLOR. The structure is well-defined except for N-terminal residues 4-6 and C-terminal residues 67-72. The rms distribution about the average structure for residues 7-66 is 0.38 A for the backbone atoms and 0.87 A for all heavy atoms. The structure consists of a series of turns and loops followed by a triple-stranded beta sheet and a C-terminal alpha helix. The structure of the monomer is largely similar to the native dimeric IL-8 structures previously determined by both NMR and X-ray methods. The major difference is that, in the monomeric analog, the C-terminal residues 67-72 are disordered whereas they are helical in the two dimeric structures. The best fit superposition of the backbone atoms of residues 7-66 of the monomer structure on the dimeric IL-8 structures showed rms differences of 1.5 and 1.2 A respectively. The turn (residues 31-35), which is disulfide linked to the N-terminal region, adopts a conformation in the monomer similar to that seen in the dimeric X-ray structure (rms difference 1.4 A) and different from that seen in the dimeric NMR structure (rms difference 2.7 A).(ABSTRACT TRUNCATED AT 250 WORDS)
+The line below this paragraph, {{ABSTRACT_PUBMED_7548056}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7548056 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7548056}}
 ==About this Structure==
-IKM 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=1IKM OCA].
+IKM 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=1IKM OCA].
 ==Reference==
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 [[Category: Rajarathnam, K.]]
 [[Category: Sykes, B D.]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 13:24:00 2008''