1kiv: Difference between revisions
New page: left|200px<br /> <applet load="1kiv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kiv, resolution 2.1Å" /> '''RECOMBINANT KRINGLE ... |
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==About this Structure== | ==About this Structure== | ||
1KIV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KIV OCA]]. | 1KIV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Structure known Active Site: LBS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KIV OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: lysine binding site]] | [[Category: lysine binding site]] | ||
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Revision as of 12:32, 30 October 2007
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RECOMBINANT KRINGLE IV-10/M66 VARIANT OF HUMAN APOLIPOPROTEIN(A)
OverviewOverview
The kringle modules of apolipoprotein(a) [apo(a)] of lipoprotein(a), [Lp(a)] are highly homologous with kringle 4 of plasminogen (75-94%) and, like the latter are autonomous structural and functional units. Apo(a), contains 14-37 kringle 4 (KIV) repeats distributed into 10 classes (1-10)., Lp(a) binds lysine-Sepharose via a lysine binding site (LBS) located in, KIV-10 (88% homology with plasminogen K4). However, the W72R substitution, that occurs in rhesus monkeys and occasionally in humans leads to impaired, lysine binding capacity of KIV-10 and Lp(a). The foregoing has been, investigated by determining the structures of KIV-10/M66 (M66 variant) in, its unliganded and ligand [epsilon-aminocaproic acid (EACA)] bound modes, and the structure of recombinant KIV-10/M66R72 (the W72R mutant). ... [(full description)]
About this StructureAbout this Structure
1KIV is a [Single protein] structure of sequence from [Homo sapiens]. Structure known Active Site: LBS. Full crystallographic information is available from [OCA].
ReferenceReference
Recombinant kringle IV-10 modules of human apolipoprotein(a): structure, ligand binding modes, and biological relevance., Mochalkin I, Cheng B, Klezovitch O, Scanu AM, Tulinsky A, Biochemistry. 1999 Feb 16;38(7):1990-8. PMID:10026282
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