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{{Theoretical_model}} | |||
==WHEY ACIDIC PROTEIN (WAP) FROM PIG (SUS SCROFA)== | |||
<StructureSection load='1cjh' size='340' side='right'caption='[[1cjh]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJH FirstGlance]. <br> | |||
</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=1cjh FirstGlance], [https://www.ebi.ac.uk/pdbsum/1cjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjh ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Whey acidic proteins (WAP) from the mouse, rat, rabbit, camel, and pig comprise two "four-disulfide core" domains. From a detailed analysis of all sequences containing this domain, we propose a new PROSITE motif ([KRHGVLN]-X- inverted question markPF inverted question mark-X-[CF]-[PQSVLI]-X(9,19)-C- inverted question markP inverted question mark-X-[DN]-X- inverted question markN inverted question mark -[CE]-X(5)-C-C) to accurately identify new four-disulfide core proteins. A consensus model for the WAP proteins is proposed, based on the human mucous proteinase inhibitor crystal structure. This article presents a detailed atomic model for the two-domain porcine WAP sequence by comparative modeling. Surface electrostatic potential calculations indicate that the second domain of the pig WAP model is similar to the functional human mucous proteinase inhibitor domains, whereas the first domain may be nonfunctional. | |||
The whey acidic protein family: a new signature motif and three-dimensional structure by comparative modeling.,Ranganathan S, Simpson KJ, Shaw DC, Nicholas KR J Mol Graph Model. 1999 Apr;17(2):106-13, 134-6. PMID:10680116<ref>PMID:10680116</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cjh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Nicholas, K R]] | |||
[[Category: Ranganathan, S]] | |||
[[Category: Shaw, D C]] | |||
[[Category: Simpson, K J]] | |||
Latest revision as of 13:37, 14 July 2021
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WHEY ACIDIC PROTEIN (WAP) FROM PIG (SUS SCROFA)WHEY ACIDIC PROTEIN (WAP) FROM PIG (SUS SCROFA)
Structural highlights
Publication Abstract from PubMedWhey acidic proteins (WAP) from the mouse, rat, rabbit, camel, and pig comprise two "four-disulfide core" domains. From a detailed analysis of all sequences containing this domain, we propose a new PROSITE motif ([KRHGVLN]-X- inverted question markPF inverted question mark-X-[CF]-[PQSVLI]-X(9,19)-C- inverted question markP inverted question mark-X-[DN]-X- inverted question markN inverted question mark -[CE]-X(5)-C-C) to accurately identify new four-disulfide core proteins. A consensus model for the WAP proteins is proposed, based on the human mucous proteinase inhibitor crystal structure. This article presents a detailed atomic model for the two-domain porcine WAP sequence by comparative modeling. Surface electrostatic potential calculations indicate that the second domain of the pig WAP model is similar to the functional human mucous proteinase inhibitor domains, whereas the first domain may be nonfunctional. The whey acidic protein family: a new signature motif and three-dimensional structure by comparative modeling.,Ranganathan S, Simpson KJ, Shaw DC, Nicholas KR J Mol Graph Model. 1999 Apr;17(2):106-13, 134-6. PMID:10680116[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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