1irp

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[[Image:1irp.png|left|200px]]
 
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{{STRUCTURE_1irp| PDB=1irp | SCENE= }}
{{STRUCTURE_1irp| PDB=1irp | SCENE= }}
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===SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN===
===SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN===
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{{ABSTRACT_PUBMED_8045306}}
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{{ABSTRACT_PUBMED_8045306}}
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==Disease==
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[[http://www.uniprot.org/uniprot/IL1RA_HUMAN IL1RA_HUMAN]] Genetic variation in IL1RN is associated with susceptibility to microvascular complications of diabetes type 4 (MVCD4) [MIM:[http://omim.org/entry/612628 612628]]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in IL1RN are the cause of interleukin 1 receptor antagonist deficiency (DIRA) [MIM:[http://omim.org/entry/612852 612852]]; also known as deficiency of interleukin 1 receptor antagonist. Autoinflammatory diseases manifest inflammation without evidence of infection, high-titer autoantibodies, or autoreactive T-cells. DIRA is a rare, autosomal recessive, genetic autoinflammatory disease that results in sterile multifocal osteomyelitis (bone inflammation in multiple places), periostitis (inflammation of the membrane surrounding the bones), and pustulosis (due to skin inflammation) from birth.<ref>PMID:19494218</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/IL1RA_HUMAN IL1RA_HUMAN]] Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling. Has no interleukin-1 like activity. Binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unsure.<ref>PMID:7775431</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:008045306</ref><references group="xtra"/>
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<ref group="xtra">PMID:008045306</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Scahill, T A.]]
[[Category: Scahill, T A.]]

Revision as of 17:49, 24 March 2013

Template:STRUCTURE 1irp

Contents

SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN

Template:ABSTRACT PUBMED 8045306

Disease

[IL1RA_HUMAN] Genetic variation in IL1RN is associated with susceptibility to microvascular complications of diabetes type 4 (MVCD4) [MIM:612628]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in IL1RN are the cause of interleukin 1 receptor antagonist deficiency (DIRA) [MIM:612852]; also known as deficiency of interleukin 1 receptor antagonist. Autoinflammatory diseases manifest inflammation without evidence of infection, high-titer autoantibodies, or autoreactive T-cells. DIRA is a rare, autosomal recessive, genetic autoinflammatory disease that results in sterile multifocal osteomyelitis (bone inflammation in multiple places), periostitis (inflammation of the membrane surrounding the bones), and pustulosis (due to skin inflammation) from birth.[1]

Function

[IL1RA_HUMAN] Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling. Has no interleukin-1 like activity. Binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unsure.[2]

About this Structure

1irp is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

See Also

Reference

  • Stockman BJ, Scahill TA, Strakalaitis NA, Brunner DP, Yem AW, Deibel MR Jr. Solution structure of human interleukin-1 receptor antagonist protein. FEBS Lett. 1994 Jul 25;349(1):79-83. PMID:8045306
  1. Aksentijevich I, Masters SL, Ferguson PJ, Dancey P, Frenkel J, van Royen-Kerkhoff A, Laxer R, Tedgard U, Cowen EW, Pham TH, Booty M, Estes JD, Sandler NG, Plass N, Stone DL, Turner ML, Hill S, Butman JA, Schneider R, Babyn P, El-Shanti HI, Pope E, Barron K, Bing X, Laurence A, Lee CC, Chapelle D, Clarke GI, Ohson K, Nicholson M, Gadina M, Yang B, Korman BD, Gregersen PK, van Hagen PM, Hak AE, Huizing M, Rahman P, Douek DC, Remmers EF, Kastner DL, Goldbach-Mansky R. An autoinflammatory disease with deficiency of the interleukin-1-receptor antagonist. N Engl J Med. 2009 Jun 4;360(23):2426-37. doi: 10.1056/NEJMoa0807865. PMID:19494218 doi:10.1056/NEJMoa0807865
  2. Greenfeder SA, Nunes P, Kwee L, Labow M, Chizzonite RA, Ju G. Molecular cloning and characterization of a second subunit of the interleukin 1 receptor complex. J Biol Chem. 1995 Jun 9;270(23):13757-65. PMID:7775431

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