Structural aspects of luteinizing hormone receptor - Information from molecular modeling and mutagenesis

被引：14

作者：

Fanelli, F

Puett, D

机构：

[1] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA

[2] Univ Modena, DTI, I-41100 Modena, Italy

[3] Univ Modena, Dept Chem, I-41100 Modena, Italy

来源：

ENDOCRINE | 2002年 / 18卷 / 03期

关键词：

lutropin receptor; G protein-coupled receptor; molecular modeling; mutagenesis; luteinizing hormone receptor;

D O I：

10.1385/ENDO:18:3:285

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

The luteinizing hormone receptor (LHR) is a member of the superfamily of G protein-coupled receptors and, in humans, binds two closely related ligands, members of the heterodimeric glycoprotein hormone family. This receptor is an essential component of the reproductive axis in males and females, and a number of naturally occurring pathophysiologic activating and inactivating mutations have been described. This review deals with the current state of knowledge of the structure of LHR based on molecular modeling and the supporting experimental data from engineered and naturally occurring mutations.

引用

收藏

页码：285 / 293

页数：9

相关论文

共 51 条

[1] Evidence for the direct involvement of transmembrane region 6 of the lutropin/choriogonadotropin receptor in activating G(S) [J].

Abell, AN ;

Segaloff, DL .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (23) :14586-14591

[2] A model for constitutive lutropin receptor activation based on molecular simulation and engineered mutations in transmembrane helices 6 and 7 [J].

Angelova, K ;

Fanelli, F ;

Puett, D .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (35) :32202-32213

[3] The lutropin/choriocrctnadotropin receptor, a 2002 perspective [J].

Ascoli, M ;

Fanelli, F ;

Segaloff, DL .

ENDOCRINE REVIEWS, 2002, 23 (02) :141-174

[4] An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors [J].

Baldwin, JM ;

Schertler, GFX ;

Unger, VM .

JOURNAL OF MOLECULAR BIOLOGY, 1997, 272 (01) :144-164

[5] Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone chorionic gonadotropin receptor by site-directed mutagenesis and modeling [J].

Bhowmick, N ;

Huang, JN ;

Puett, D ;

Isaacs, NW ;

Lapthorn, AJ .

MOLECULAR ENDOCRINOLOGY, 1996, 10 (09) :1147-1159

[6] Identification of ionizable amino acid residues on the extracellular domain of the lutropin receptor involved in ligand binding [J].

Bhowmick, N ;

Narayan, P ;

Puett, D .

ENDOCRINOLOGY, 1999, 140 (10) :4558-4563

[7] CHARMM - A PROGRAM FOR MACROMOLECULAR ENERGY, MINIMIZATION, AND DYNAMICS CALCULATIONS [J].

BROOKS, BR ;

BRUCCOLERI, RE ;

OLAFSON, BD ;

STATES, DJ ;

SWAMINATHAN, S ;

KARPLUS, M .

JOURNAL OF COMPUTATIONAL CHEMISTRY, 1983, 4 (02) :187-217

[8] Structure/function relationships of a G-protein coupling pocket formed by the third intracellular loop of the m5 muscarinic receptor [J].

Burstein, ES ;

Spalding, TA ;

Brann, MR .

BIOCHEMISTRY, 1998, 37 (12) :4052-4058

[9] The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling [J].

Burstein, ES ;

Spalding, TA ;

Brann, MR .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (38) :24322-24327

[10] THE RELATION BETWEEN THE DIVERGENCE OF SEQUENCE AND STRUCTURE IN PROTEINS [J].

CHOTHIA, C ;

LESK, AM .

EMBO JOURNAL, 1986, 5 (04) :823-826

← 1 2 3 4 5 6 →